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Conserved domains on  [gi|482661637|ref|NP_001264796|]
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M-phase phosphoprotein 9 isoform a [Mus musculus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 573-754 5.18e-08

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 57.34  E-value: 5.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   573 YESEISSLKQKLEAKDISAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRerfNAASSASKVLQ 652
Cdd:TIGR04523  293 LKSEISDLNNQKEQDWNKELKSELKNQE---KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQRELE 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   653 ERIEEMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTE 729
Cdd:TIGR04523  367 EKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446

                          170       180
                   ....*....|....*....|....*
gi 482661637   730 NKLLDAHTQISDLKRTISKLEAQVK 754
Cdd:TIGR04523  447 NQDSVKELIIKNLDNTRESLETQLK 471
 
Name Accession Description Interval E-value
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 573-754 5.18e-08

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 57.34  E-value: 5.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   573 YESEISSLKQKLEAKDISAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRerfNAASSASKVLQ 652
Cdd:TIGR04523  293 LKSEISDLNNQKEQDWNKELKSELKNQE---KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQRELE 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   653 ERIEEMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTE 729
Cdd:TIGR04523  367 EKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446

                          170       180
                   ....*....|....*....|....*
gi 482661637   730 NKLLDAHTQISDLKRTISKLEAQVK 754
Cdd:TIGR04523  447 NQDSVKELIIKNLDNTRESLETQLK 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 551-759 1.39e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  551 LSKIRQNLKEKHARHVADLRAYYESEISSLKQKLEAKdISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLL 630
Cdd:COG1196   222 LKELEAELLLLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  631 EIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGE 710
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 482661637  711 YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
551-757 6.98e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  551 LSKIRQNLKE-----KHARHVADLRAYYEsEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLD---SALNEATSRVRT 622
Cdd:PRK03918  475 ERKLRKELRElekvlKKESELIKLKELAE-QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKLEE 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  623 LEKNNNLLEIEVSDLRERF--------NAASSASKVLQERIEEMR----------TSNKEKDNTITRLKCRLQDLEEAFE 684
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELaellkeleELGFESVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  685 NAYKLSDD---KEARLRQENKMFQD-----LLGEYESLGKEHGRVKDTLNTTENklldahtQISDLKRTISKLEAQVKQA 756
Cdd:PRK03918  634 ELAETEKRleeLRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEK-------RREEIKKTLEKLKEELEER 706


                  .
gi 482661637  757 E 757
Cdd:PRK03918  707 E 707
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 577-749 9.82e-06

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: 49.82  E-value: 9.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   577 ISSLKQKLEAKDISAvEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIE 656
Cdd:pfam10174  326 IEVLKESLTAKEQRA-AILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   657 EMRTSNKEKDNTITRLKCRLQDLEE----------AFENAykLSDDK---EARLRQENKMFQDLLGEYESLGKEHGRVKD 723
Cdd:pfam10174  405 NLQEQLRDKDKQLAGLKERVKSLQTdssntdtaltTLEEA--LSEKEriiERLKEQREREDRERLEELESLKKENKDLKE 482

                          170       180
                   ....*....|....*....|....*.
gi 482661637   724 TLNTTENKLLDAHTQISDLKRTISKL 749
Cdd:pfam10174  483 KVSALQPELTEKESSLIDLKEHASSL 508
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 594-765 5.27e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.47  E-value: 5.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637    594 EWKKKneILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMrtsNKEKDNTITRLK 673
Cdd:smart00787  136 EWRMK--LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDEL---EDCDPTELDRAK 210

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637    674 CRLQDLEEAFENAYKLSDDKEARLRQenkmfqdllgeyeslgkehgrVKDTLNTTENKLLDAHTQISDLKRT-------- 745
Cdd:smart00787  211 EKLKKLLQEIMIKVKKLEELEEELQE---------------------LESKIEDLTNKKSELNTEIAEAEKKleqcrgft 269

                           170       180
                    ....*....|....*....|...
gi 482661637    746 ---ISKLEAQVKQAEHESMLSLR 765
Cdd:smart00787  270 fkeIEKLKEQLKLLQSLTGWKIT 292
 
Name Accession Description Interval E-value
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 573-754 5.18e-08

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 57.34  E-value: 5.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   573 YESEISSLKQKLEAKDISAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRerfNAASSASKVLQ 652
Cdd:TIGR04523  293 LKSEISDLNNQKEQDWNKELKSELKNQE---KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQRELE 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   653 ERIEEMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTE 729
Cdd:TIGR04523  367 EKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446

                          170       180
                   ....*....|....*....|....*
gi 482661637   730 NKLLDAHTQISDLKRTISKLEAQVK 754
Cdd:TIGR04523  447 NQDSVKELIIKNLDNTRESLETQLK 471
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 575-761 7.28e-08

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 56.95  E-value: 7.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   575 SEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLdSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQER 654
Cdd:TIGR04523  162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   655 IEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKE-----HGRVKDTLNTTE 729
Cdd:TIGR04523  241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQE 320

                          170       180       190
                   ....*....|....*....|....*....|..
gi 482661637   730 NKLLDAHTQISDLKRTISKLEAQVKQAEHESM 761
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 551-757 7.33e-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: 56.99  E-value: 7.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   551 LSKIRQNLKEKHARHVADLRAYYESEISSLKQKLEAKDiSAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKN---- 626
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELE-EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqil 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   627 --------NNLLEIEVS---------DLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKL 689
Cdd:TIGR02168  308 rerlanleRQLEELEAQleeleskldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 482661637   690 SDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNT-----TENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLE 460
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 551-759 1.39e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  551 LSKIRQNLKEKHARHVADLRAYYESEISSLKQKLEAKdISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLL 630
Cdd:COG1196   222 LKELEAELLLLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  631 EIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGE 710
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 482661637  711 YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 580-759 3.93e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  580 LKQKLEAKDIS-AVEEWKKKNEILAdrcgQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEM 658
Cdd:COG1196   218 LKEELKELEAElLLLKLRELEAELE----ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  659 RTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQ 738
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                         170       180
                  ....*....|....*....|.
gi 482661637  739 ISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1196   374 LAEAEEELEELAEELLEALRA 394
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 608-759 7.56e-07

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.46  E-value: 7.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  608 QLDSALNEATSRVRTLEKnnnlleiEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAY 687
Cdd:COG1579    14 ELDSELDRLEHRLKELPA-------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 482661637  688 KlsddkearlrqeNKMFQDLLGEYESLGKEhgrvkdtLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1579    87 N------------NKEYEALQKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEAE 139
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 593-757 1.13e-06

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: 53.15  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   593 EEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRL 672
Cdd:TIGR02169  684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   673 KCRLQDLEEAFENAYKLSDDKEARLRQEnkMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQ 752
Cdd:TIGR02169  764 EARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841


                   ....*
gi 482661637   753 VKQAE 757
Cdd:TIGR02169  842 RIDLK 846
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 574-732 4.65e-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: 51.21  E-value: 4.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   574 ESEISSLKQKLEaKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQE 653
Cdd:TIGR02168  781 EAEIEELEAQIE-QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 482661637   654 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKL 732
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
551-757 6.98e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  551 LSKIRQNLKE-----KHARHVADLRAYYEsEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLD---SALNEATSRVRT 622
Cdd:PRK03918  475 ERKLRKELRElekvlKKESELIKLKELAE-QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKLEE 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  623 LEKNNNLLEIEVSDLRERF--------NAASSASKVLQERIEEMR----------TSNKEKDNTITRLKCRLQDLEEAFE 684
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELaellkeleELGFESVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  685 NAYKLSDD---KEARLRQENKMFQD-----LLGEYESLGKEHGRVKDTLNTTENklldahtQISDLKRTISKLEAQVKQA 756
Cdd:PRK03918  634 ELAETEKRleeLRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEK-------RREEIKKTLEKLKEELEER 706


                  .
gi 482661637  757 E 757
Cdd:PRK03918  707 E 707
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
576-762 8.30e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 8.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  576 EISSLKQKLEAKDiSAVEEWKKKNEILAdrcgQLDSALNEATSRVRTLEKNNNLLE--IEVSDLRERFNAASSASKVLQE 653
Cdd:COG4717    72 ELKELEEELKEAE-EKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  654 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQEnkmFQDLLGEYESLGKEHGRVKDTLNTTENKLL 733
Cdd:COG4717   147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELE 223

                         170       180
                  ....*....|....*....|....*....
gi 482661637  734 DAHTQISDLKRTISKLEAQVKQAEHESML 762
Cdd:COG4717   224 ELEEELEQLENELEAAALEERLKEARLLL 252
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 577-749 9.82e-06

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: 49.82  E-value: 9.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   577 ISSLKQKLEAKDISAvEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIE 656
Cdd:pfam10174  326 IEVLKESLTAKEQRA-AILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   657 EMRTSNKEKDNTITRLKCRLQDLEE----------AFENAykLSDDK---EARLRQENKMFQDLLGEYESLGKEHGRVKD 723
Cdd:pfam10174  405 NLQEQLRDKDKQLAGLKERVKSLQTdssntdtaltTLEEA--LSEKEriiERLKEQREREDRERLEELESLKKENKDLKE 482

                          170       180
                   ....*....|....*....|....*.
gi 482661637   724 TLNTTENKLLDAHTQISDLKRTISKL 749
Cdd:pfam10174  483 KVSALQPELTEKESSLIDLKEHASSL 508
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 574-759 1.07e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.63  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   574 ESEISSLKQKLEAKDiSAVEEWKKKNEILADRCGQLDSALNEATS--------------RVRTLEKNNNLLEIEVSDLRE 639
Cdd:TIGR04523  355 ESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESkiqnqeklnqqkdeQIKKLQQEKELLEKEIERLKE 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   640 RFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLgkehg 719
Cdd:TIGR04523  434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL----- 508

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 482661637   720 rvkdtlnttENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:TIGR04523  509 ---------EEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
554-778 1.09e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  554 IRQNLKEKHARhVADLRAYYESEISSLKQKLEAKDiSAVEEWKKKNEI----------------LADRCGQLDSALNEAT 617
Cdd:COG3206   162 LEQNLELRREE-ARKALEFLEEQLPELRKELEEAE-AALEEFRQKNGLvdlseeaklllqqlseLESQLAEARAELAEAE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  618 SRVRTLEKNNNL-----------------------LEIEVSDLRERFNAASSASKVLQERIEEMRTS-NKEKDNTITRLK 673
Cdd:COG3206   240 ARLAALRAQLGSgpdalpellqspviqqlraqlaeLEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLE 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  674 CRLQDLEEAfENAYKlsdDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLldahtqisdlkrtiskLEAQV 753
Cdd:COG3206   320 AELEALQAR-EASLQ---AQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL----------------EEARL 379

                         250       260
                  ....*....|....*....|....*
gi 482661637  754 KQAEHESMLSLRNGAKVPERPSRSN 778
Cdd:COG3206   380 AEALTVGNVRVIDPAVVPLKPVSPK 404
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
560-757 1.17e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  560 EKHARHVADLRAYYESEISSLKQKLEAKdiSAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRE 639
Cdd:PRK03918  161 ENAYKNLGEVIKEIKRRIERLEKFIKRT--ENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELEE 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  640 RFnaassaskvlqERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMfQDLLGEYESLGKEHG 719
Cdd:PRK03918  236 LK-----------EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYE 303

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 482661637  720 RVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:PRK03918  304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 551-757 1.21e-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: 49.68  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   551 LSKIRQNLKEKHARHVADLrAYYESEISSLKQKLEA-KDISAVEEWKKKN---EILADRCGQLDSALNEATSRVRTLEKN 626
Cdd:TIGR02169  749 LEQEIENVKSELKELEARI-EELEEDLHKLEEALNDlEARLSHSRIPEIQaelSKLEEEVSRIEARLREIEQKLNRLTLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   627 NNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEafenayKLSDDKEARLRQENKMfqd 706
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES------RLGDLKKERDELEAQL--- 898

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 482661637   707 llgeyeslgkehGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:TIGR02169  899 ------------RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 573-759 1.25e-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: 49.67  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   573 YESEISSLKQKLEAKD--ISAVEEwkkKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKV 650
Cdd:TIGR02168  244 LQEELKEAEEELEELTaeLQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   651 LQERIEemrtsnkEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTEN 730
Cdd:TIGR02168  321 LEAQLE-------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393

                          170       180
                   ....*....|....*....|....*....
gi 482661637   731 KLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQE 422
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 550-757 1.96e-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: 48.90  E-value: 1.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   550 MLSKIRQNLKEKHARHVAdlrAYYESEISSLKQKLEAKDIS----AVEEWKKKNEILADRCGQLDSALNEA-------TS 618
Cdd:TIGR02168  713 ELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAqlskELTELEAEIEELEERLEEAEEELAEAeaeieelEA 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   619 RVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLR 698
Cdd:TIGR02168  790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 482661637   699 QENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:TIGR02168  870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 555-755 3.02e-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: 48.51  E-value: 3.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   555 RQNLKEKHARHVADLRAYYESEISSLKQKLEaKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEV 634
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   635 SDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESL 714
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 482661637   715 GKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQ 755
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 567-757 3.75e-05

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: 47.45  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  567 ADLRAYYESEISSLKQKLEAKDISAVEEWKKKNEILADRcGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASS 646
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  647 ASKVLQERIEEM-----RTSN------------------------------KEKDNTITRLKCRLQDLEEAFENAYKLSD 691
Cdd:COG4942    98 ELEAQKEELAELlralyRLGRqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAERAELE 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 482661637  692 DKEARLRQENKMFQDLLGEYESLGKehgRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
569-772 6.13e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 6.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  569 LRAYYES--EISSLKQKLEaKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASS 646
Cdd:PRK02224  243 LEEHEERreELETLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  647 ASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEE--------------AFENAYKLSDDKEARLRQENKMFQDLLGEYE 712
Cdd:PRK02224  322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreeaaelesELEEAREAVEDRREEIEELEEEIEELRERFG 401

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  713 SLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEhesmlSLRNGAKVPE 772
Cdd:PRK02224  402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE-----ALLEAGKCPE 456
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 550-817 1.00e-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: 46.60  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   550 MLSKIRQNLkEKHARHVADLRAYyeSEISSLKQKLEAKDISAveEWKKKNEILADRCGQLDSA---LNEATSRVRTLEKN 626
Cdd:TIGR02169  192 IIDEKRQQL-ERLRREREKAERY--QALLKEKREYEGYELLK--EKEALERQKEAIERQLASLeeeLEKLTEEISELEKR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   627 NNLLEIEVSDLRERFNAASSASKV-LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQ 705
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   706 DLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHESMLSLRNGAKVPERPSRsnsvATSDV 785
Cdd:TIGR02169  347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR----LSEEL 422

                          250       260       270
                   ....*....|....*....|....*....|..
gi 482661637   786 SRRKWLIPGAEysiftGQPLDPRDRKLDKQLE 817
Cdd:TIGR02169  423 ADLNAAIAGIE-----AKINELEEEKEDKALE 449
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 551-759 1.44e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  551 LSKIRQNLKEKHARHVADLRAYyESEISSLKQKLEAKDIsAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLL 630
Cdd:COG1196   244 LEAELEELEAELEELEAELAEL-EAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  631 EIEVSDLRERFNAassaskvLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGE 710
Cdd:COG1196   322 EEELAELEEELEE-------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 482661637  711 YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 602-757 1.64e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.53  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  602 LADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMR------TSNKEKDN---TITRL 672
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKEYEAlqkEIESL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  673 KCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEhgrvkdtlnttenklLDAhtQISDLKRTISKLEAQ 752
Cdd:COG1579   102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---------------LDE--ELAELEAELEELEAE 164


                  ....*
gi 482661637  753 VKQAE 757
Cdd:COG1579   165 REELA 169
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 551-714 2.11e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  551 LSKIRQNLKEkHARHVADLrayyESEISSLKQKLEA--KDISAVEEWKKKNEILADrcgQLDSALNEATSRVRTLEKNNN 628
Cdd:COG1579    19 LDRLEHRLKE-LPAELAEL----EDELAALEARLEAakTELEDLEKEIKRLELEIE---EVEARIKKYEEQLGNVRNNKE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  629 L--LEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE-----N 701
Cdd:COG1579    91 YeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEreelaA 170

                         170
                  ....*....|...
gi 482661637  702 KMFQDLLGEYESL 714
Cdd:COG1579   171 KIPPELLALYERI 183
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
552-757 2.55e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  552 SKIRQNLKEKHARHVADLRAYyeSEISSLKQKLEAKdISAVEEWKKKNEILADRcgqldsaLNEATSRVRTLEKNNNLLE 631
Cdd:PRK03918  189 ENIEELIKEKEKELEEVLREI--NEISSELPELREE-LEKLEKEVKELEELKEE-------IEELEKELESLEGSKRKLE 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  632 IEVSDLRERFNAASSASKVLQERI----------EEMRTSNKEKDNT---ITRLKCRLQDLEEAFENAYKLSDD---KEA 695
Cdd:PRK03918  259 EKIRELEERIEELKKEIEELEEKVkelkelkekaEEYIKLSEFYEEYldeLREIEKRLSRLEEEINGIEERIKEleeKEE 338

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 482661637  696 RLRQENKMFQDLLGEYESLGKEHgRVKDTLNTTENKLLDAHTQISDLkrTISKLEAQVKQAE 757
Cdd:PRK03918  339 RLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELE 397
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
566-755 4.14e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  566 VADLRAYYESEISSLKQK---LEAkDISAVEEWKKKNEILAD-----RCGQ--LDS----ALNEATSRVRTLEKNNNLLE 631
Cdd:PRK02224  410 AEDFLEELREERDELREReaeLEA-TLRTARERVEEAEALLEagkcpECGQpvEGSphveTIEEDRERVEELEAELEDLE 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  632 IEVSDLRERFNAASSASKV-------------LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAfenayklSDDKEARLR 698
Cdd:PRK02224  489 EEVEEVEERLERAEDLVEAedrierleerredLEELIAERRETIEEKRERAEELRERAAELEAE-------AEEKREAAA 561

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 482661637  699 QENKMFQDLLGEYESLGKEHGRVKDTLNTTeNKLLDAHTQISDLKRTISKLEAQVKQ 755
Cdd:PRK02224  562 EAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREA 617
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 633-760 4.45e-04

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 42.58  E-value: 4.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   633 EVSDLRERFnaassasKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEeafenayKLSDDK---------------EARL 697
Cdd:pfam15619   68 EVRVLRERL-------RRLQEKERDLERKLKEKEAELLRLRDQLKRLE-------KLSEDKnlaereelqkkleqlEAKL 133

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 482661637   698 RQENKMFQDLLGEYESLGKEHGRvkdTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHES 760
Cdd:pfam15619  134 EDKDEKIQDLERKLELENKSFRR---QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 594-765 5.27e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.47  E-value: 5.27e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637    594 EWKKKneILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMrtsNKEKDNTITRLK 673
Cdd:smart00787  136 EWRMK--LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDEL---EDCDPTELDRAK 210

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637    674 CRLQDLEEAFENAYKLSDDKEARLRQenkmfqdllgeyeslgkehgrVKDTLNTTENKLLDAHTQISDLKRT-------- 745
Cdd:smart00787  211 EKLKKLLQEIMIKVKKLEELEEELQE---------------------LESKIEDLTNKKSELNTEIAEAEKKleqcrgft 269

                           170       180
                    ....*....|....*....|...
gi 482661637    746 ---ISKLEAQVKQAEHESMLSLR 765
Cdd:smart00787  270 fkeIEKLKEQLKLLQSLTGWKIT 292
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
633-759 5.42e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  633 EVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQEN-------KMFQ 705
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeelqEELE 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 482661637  706 DLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG4372   119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
566-756 6.33e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  566 VADLRAYYESEISSLKQKLEAKDISA-------------VEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEI 632
Cdd:PRK02224  312 VEARREELEDRDEELRDRLEECRVAAqahneeaeslredADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  633 EVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAyklsddkeARLRQENK---MFQDLLG 709
Cdd:PRK02224  392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA--------EALLEAGKcpeCGQPVEG 463

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 482661637  710 EYESLGKEHGRVKdtLNTTENKLLDAHTQISDLKRTISKLEAQVKQA 756
Cdd:PRK02224  464 SPHVETIEEDRER--VEELEAELEDLEEEVEEVEERLERAEDLVEAE 508
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 557-759 8.06e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 8.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   557 NLKEKHARHVADLRAYYESEISSLKQKLEAKDISaVEEWKKKNEILADrcgQLDSALNEATSRVRTLEKNNNLLEIEVSD 636
Cdd:TIGR04523  422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI-IKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKE 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   637 LRERFNAASSAS---KVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFE--NAYKLSDDKEARLRQENKMFQDLLGEY 711
Cdd:TIGR04523  498 LKKLNEEKKELEekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQTQ 577

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 482661637   712 ESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:TIGR04523  578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
Filament pfam00038
Intermediate filament protein;
619-700 8.11e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 42.99  E-value: 8.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   619 RVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQER-IEEMRtsNKEKDNTITRLKCRLQ--DLEEAFENaYKLSDDKEA 695
Cdd:pfam00038   19 KVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKeIEDLR--RQLDTLTVERARLQLEldNLRLAAED-FRQKYEDEL 95


                   ....*
gi 482661637   696 RLRQE 700
Cdd:pfam00038   96 NLRTS 100
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
563-763 8.24e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  563 ARHVADLRAYYESEISSLKQKLEAKDISAVEEWKKkneiLADRCGQLDSALNEATSRVRTLEKNNnlLEIEVSDLRERFN 642
Cdd:COG4717   307 LQALPALEELEEEELEELLAALGLPPDLSPEELLE----LLDRIEELQELLREAEELEEELQLEE--LEQEIAALLAEAG 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  643 AASSASkvLQERIEEMRtsnkekdntitrlkcRLQDLEEAFENAyklsddkEARLRQENKMFQDLLgeyESLGKEhgRVK 722
Cdd:COG4717   381 VEDEEE--LRAALEQAE---------------EYQELKEELEEL-------EEQLEELLGELEELL---EALDEE--ELE 431

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 482661637  723 DTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHESMLS 763
Cdd:COG4717   432 EELEELEEELEELEEELEELREELAELEAELEQLEEDGELA 472
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
592-766 9.85e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 9.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  592 VEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERfnaASSASKVLQERIEEMRTSNKEKDNTITR 671
Cdd:COG1340    10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE---AQELREKRDELNEKVKELKEERDELNEK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  672 LKCRLQDLEEAFENAYKLSDDK------EARLRQENKMFQ----------DLLGEYESLGKEHGRVKDtLNTTENKLLDA 735
Cdd:COG1340    87 LNELREELDELRKELAELNKAGgsidklRKEIERLEWRQQtevlspeeekELVEKIKELEKELEKAKK-ALEKNEKLKEL 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 482661637  736 HTQISDLKRTISKLEAQVK------QAEHESMLSLRN 766
Cdd:COG1340   166 RAELKELRKEAEEIHKKIKelaeeaQELHEEMIELYK 202
PRK09039 PRK09039
peptidoglycan -binding protein;
610-744 1.20e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  610 DSALNEATSRVR------TLEKNNNL-LEIEVSDLRERFNAASSaskvLQERIEEMRTsnkEKDNTITRLKCRLQDLEEA 682
Cdd:PRK09039   52 DSALDRLNSQIAeladllSLERQGNQdLQDSVANLRASLSAAEA----ERSRLQALLA---ELAGAGAAAEGRAGELAQE 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 482661637  683 FENAYKLSDDKEARLrqenkmfqDLLGE-YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKR 744
Cdd:PRK09039  125 LDSEKQVSARALAQV--------ELLNQqIAALRRQLAALEAALDASEKRDRESQAKIADLGR 179
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
551-711 1.68e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  551 LSKIRQNLKEKHARHVADLrayyESEISSL----KQKLEAKDI-SAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEK 625
Cdd:PRK03918  572 LAELLKELEELGFESVEEL----EERLKELepfyNEYLELKDAeKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  626 NNNLLEIEVSD-----LRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKE--ARLR 698
Cdd:PRK03918  648 ELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALErvEELR 727

                         170
                  ....*....|...
gi 482661637  699 QENKMFQDLLGEY 711
Cdd:PRK03918  728 EKVKKYKALLKER 740
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 651-759 2.04e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   651 LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMF-------QDLLGEYESLGKEHGRVKD 723
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaevEQLEERIAQLSKELTELEA 761

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 482661637   724 TLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
567-738 2.04e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  567 ADLRAYYESEISSLKQKLEA--KDISAVEEWKKKNEILADRCGQLDsALNEATSRVRTLEKnnnllEI-EVSDLRERFNA 643
Cdd:COG4913   609 RAKLAALEAELAELEEELAEaeERLEALEAELDALQERREALQRLA-EYSWDEIDVASAER-----EIaELEAELERLDA 682

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  644 ASSASKVLQERIE----EMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE-----NKMFQDLLGE- 710
Cdd:COG4913   683 SSDDLAALEEQLEeleaELEELEEELDelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElrallEERFAAALGDa 762

                         170       180       190
                  ....*....|....*....|....*....|...
gi 482661637  711 -----YESLGKEHGRVKDTLNTTENKLLDAHTQ 738
Cdd:COG4913   763 verelRENLEERIDALRARLNRAEEELERAMRA 795
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 541-757 3.55e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.49  E-value: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   541 SLASLEDPVMLSKIRQNlKEKHARHVADLRAYYESEISSLKQKLEAKDISAVEEWKKKNEILadrcgqldsalNEATSRV 620
Cdd:TIGR00618  664 ALSIRVLPKELLASRQL-ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE-----------NASSSLG 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   621 RTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE 700
Cdd:TIGR00618  732 SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 482661637   701 NKMFQD-LLGEYESLGKEhgrvkdtLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:TIGR00618  812 IPSDEDiLNLQCETLVQE-------EEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 574-759 3.92e-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: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  574 ESEISSLKQKLEAKDISAVEEwKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQE 653
Cdd:COG1196   301 EQDIARLEERRRELEERLEEL-EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  654 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAyklsDDKEARLRQENKMFQD----LLGEYESLGKEHGRVKDTLNTTE 729
Cdd:COG1196   380 ELEELAEELLEALRAAAELAAQLEELEEAEEAL----LERLERLEEELEELEEalaeLEEEEEEEEEALEEAAEEEAELE 455

                         170       180       190
                  ....*....|....*....|....*....|
gi 482661637  730 NKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEE 485
46 PHA02562
endonuclease subunit; Provisional
 576-759 4.16e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  576 EISSLKQKLEAKDISAVEEWKKKNEILADRCGQLDSALNEAtsrvRTLEKNNNLLEIEVSDL-RERFNAASSASKVLQER 654
Cdd:PHA02562  189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA----KTIKAEIEELTDELLNLvMDIEDPSAALNKLNTAA 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  655 IE---EMRTSNKE----KDNTItrlkCR--LQDLEEAFENAYKLSDdKEARLRQENKMFQDLLGEYESLgkehgrvKDTL 725
Cdd:PHA02562  265 AKiksKIEQFQKVikmyEKGGV----CPtcTQQISEGPDRITKIKD-KLKELQHSLEKLDTAIDELEEI-------MDEF 332

                         170       180       190
                  ....*....|....*....|....*....|....
gi 482661637  726 NTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:PHA02562  333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAA 366
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 556-773 5.41e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   556 QNLKEKHARHVADL-RAYYESEISSLKQKLEAKdiSAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEV 634
Cdd:pfam07888   33 QNRLEECLQERAELlQAQEAANRQREKEKERYK--RDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   635 SDLRERFNAASSASKVLQERIEEMRTSNK-------EKDNTITRLKCRLQDL------EEAFENAYKLS-DDKEARLRQE 700
Cdd:pfam07888  111 EELSEEKDALLAQRAAHEARIRELEEDIKtltqrvlERETELERMKERAKKAgaqrkeEEAERKQLQAKlQQTEEELRSL 190

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 482661637   701 NKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLkrtiskleaqvkQAEHESMLSLRNGAKVPER 773
Cdd:pfam07888  191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN------------EALLEELRSLQERLNASER 251
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
567-752 5.52e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  567 ADLRAY--YESEISSLKQKLEAK-DISAVeewkkKNEILAdrcGQ-LDSALNEATSRVRTLEKNNNLL-----EIEVSDL 637
Cdd:COG2433   340 AALKAYdaYKNKFERVEKKVPPDvDRDEV-----KARVIR---GLsIEEALEELIEKELPEEEPEAERekeheERELTEE 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  638 RERFnaassasKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEafenayKLsddKEARLRQENKMFQDllGEYESLGKE 717
Cdd:COG2433   412 EEEI-------RRLEEQVERLEAEVEELEAELEEKDERIERLER------EL---SEARSEERREIRKD--REISRLDRE 473

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 482661637  718 HGRVKDTLNTTENKLLDAHTQISDLKRTIsKLEAQ 752
Cdd:COG2433   474 IERLERELEEERERIEELKRKLERLKELW-KLEHS 507
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
526-661 5.76e-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: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  526 QSQLPGTANSVPECIS----------LASLEdpVMLSKIRQNLKEKHARhVADLRAyyesEISSLKQKLEAKDISAVEEW 595
Cdd:COG3206   246 RAQLGSGPDALPELLQspviqqlraqLAELE--AELAELSARYTPNHPD-VIALRA----QIAALRAQLQQEAQRILASL 318

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 482661637  596 KKKNEILADRCGQLDSALNEATSRVRTLeknnNLLEIEVSDLRERFNAASSASKVLQERIEEMRTS 661
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLEEARLA 380
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
 656-807 7.22e-03

CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129661 [Multi-domain]  Cd Length: 309  Bit Score: 39.79  E-value: 7.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637   656 EEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKL-SDDKEARLRQENKMFQDllgeyESLGKEHGRvKDTLNTTENKLLD 734
Cdd:TIGR00570  120 KKIETYQKENKDVIQKNKEKSTREQEELEEALEFeKEEEEQRRLLLQKEEEE-----QQMNKRKNK-QALLDELETSTLP 193

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 482661637   735 AHTQISDLKRTISKLEAQVKQAEHESMLSLRNGAKVPERPSRSNsvatsdvsrrkwlIPGAEYSIFTGQPLDP 807
Cdd:TIGR00570  194 AAELIAQHKKNSVKLEMQVEKPKPEKPNTFSTGIKMGYQISLVP-------------VQKSEEALYPYQPLNI 253
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
605-757 9.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  605 RCGQLDSALNEATSRVRTLEK----------NNNLLEI--EVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRL 672
Cdd:PRK03918  133 RQGEIDAILESDESREKVVRQilglddyenaYKNLGEVikEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482661637  673 KCRLQDLEEAFENayklsddkearLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQ 752
Cdd:PRK03918  213 SSELPELREELEK-----------LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281


                  ....*
gi 482661637  753 VKQAE 757
Cdd:PRK03918  282 VKELK 286
 
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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