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Conserved domains on  [gi|755513724|ref|XP_011246507|]
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M-phase phosphoprotein 9 isoform X3 [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 ...
 415-596 3.12e-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: 57.72  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  415 YESEISSLKQKLEAKDISAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRerfNAASSASKVLQ 494
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQE---KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQRELE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  495 ERIEEMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTE 571
Cdd:TIGR04523 367 EKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446

                         170       180
                  ....*....|....*....|....*
gi 755513724  572 NKLLDAHTQISDLKRTISKLEAQVK 596
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 ...
 415-596 3.12e-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: 57.72  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  415 YESEISSLKQKLEAKDISAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRerfNAASSASKVLQ 494
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQE---KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQRELE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  495 ERIEEMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTE 571
Cdd:TIGR04523 367 EKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446

                         170       180
                  ....*....|....*....|....*
gi 755513724  572 NKLLDAHTQISDLKRTISKLEAQVK 596
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLK 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 393-601 9.85e-08

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: 9.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 393 LSKIRQNLKEKHARHVADLRAYYESEISSLKQKLEAKdISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLL 472
Cdd:COG1196  222 LKELEAELLLLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 473 EIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGE 552
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755513724 553 YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 419-591 5.13e-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: 50.59  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  419 ISSLKQKLEAKDISAvEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIE 498
Cdd:pfam10174 326 IEVLKESLTAKEQRA-AILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  499 EMRTSNKEKDNTITRLKCRLQDLEE----------AFENAykLSdDKE---ARLR-QENKMFQDLLGEYESLGKEHGRVK 564
Cdd:pfam10174 405 NLQEQLRDKDKQLAGLKERVKSLQTdssntdtaltTLEEA--LS-EKEriiERLKeQREREDRERLEELESLKKENKDLK 481

                         170       180
                  ....*....|....*....|....*..
gi 755513724  565 DTLNTTENKLLDAHTQISDLKRTISKL 591
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSL 508
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
393-599 6.07e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 393 LSKIRQNLKE-----KHARHVADLRAYYEsEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLD---SALNEATSRVRT 464
Cdd:PRK03918 475 ERKLRKELRElekvlKKESELIKLKELAE-QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKLEE 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 465 LEKNNNLLEIEVSDLRERF--------NAASSASKVLQERIEEMR----------TSNKEKDNTITRLKCRLQDLEEAFE 526
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELaellkeleELGFESVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 527 NAYKLSDD---KEARLRQENKMFQD-----LLGEYESLGKEHGRVKDTLNTTENklldahtQISDLKRTISKLEAQVKQA 598
Cdd:PRK03918 634 ELAETEKRleeLRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEK-------RREEIKKTLEKLKEELEER 706


                 .
gi 755513724 599 E 599
Cdd:PRK03918 707 E 707
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 436-607 3.43e-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: 43.85  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   436 EWKKKneILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMrtsNKEKDNTITRLK 515
Cdd:smart00787 136 EWRMK--LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDEL---EDCDPTELDRAK 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   516 CRLQDLEEAFENAYKLSDDKEARLRQenkmfqdllgeyeslgkehgrVKDTLNTTENKLLDAHTQISDLKRT-------- 587
Cdd:smart00787 211 EKLKKLLQEIMIKVKKLEELEEELQE---------------------LESKIEDLTNKKSELNTEIAEAEKKleqcrgft 269

                          170       180
                   ....*....|....*....|...
gi 755513724   588 ---ISKLEAQVKQAEHESMLSLR 607
Cdd:smart00787 270 fkeIEKLKEQLKLLQSLTGWKIT 292
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 384-577 3.95e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 39.74  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 384 LASLEDPVMLSKIrQNLKEKHARHVADLRAYYE--SEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLdsaLNEATSR 461
Cdd:cd00176   23 LSSTDYGDDLESV-EALLKKHEALEAELAAHEErvEALNELGEQLIEEGHPDAEEIQERLEELNQRWEEL---RELAEER 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 462 VRTLEknnnlleiEVSDLRERFNAASSASKVLQERIEEMRTSNKEKD-NTITRLKCRLQDLEEAFENayklsddKEARLR 540
Cdd:cd00176   99 RQRLE--------EALDLQQFFRDADDLEQWLEEKEAALASEDLGKDlESVEELLKKHKELEEELEA-------HEPRLK 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755513724 541 QENKMFQDLLGEYESLGKEHGRVK-DTLNTTENKLLDA 577
Cdd:cd00176  164 SLNELAEELLEEGHPDADEEIEEKlEELNERWEELLEL 201
 
Name Accession Description Interval E-value
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 415-596 3.12e-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: 57.72  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  415 YESEISSLKQKLEAKDISAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRerfNAASSASKVLQ 494
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQE---KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQRELE 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  495 ERIEEMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTE 571
Cdd:TIGR04523 367 EKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446

                         170       180
                  ....*....|....*....|....*
gi 755513724  572 NKLLDAHTQISDLKRTISKLEAQVK 596
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLK 471
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 393-599 4.43e-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: 57.37  E-value: 4.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   393 LSKIRQNLKEKHARHVADLRAYYESEISSLKQKLEAKDiSAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKN---- 468
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELE-EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqil 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   469 --------NNLLEIEVS---------DLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKL 531
Cdd:TIGR02168  308 rerlanleRQLEELEAQleeleskldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755513724   532 SDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNT-----TENKLLDAHTQISDLKRTISKLEAQVKQAE 599
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLE 460
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 417-603 4.87e-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: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  417 SEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLdSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQER 496
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  497 IEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKE-----HGRVKDTLNTTE 571
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQE 320

                         170       180       190
                  ....*....|....*....|....*....|..
gi 755513724  572 NKLLDAHTQISDLKRTISKLEAQVKQAEHESM 603
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 393-601 9.85e-08

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: 9.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 393 LSKIRQNLKEKHARHVADLRAYYESEISSLKQKLEAKdISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLL 472
Cdd:COG1196  222 LKELEAELLLLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 473 EIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGE 552
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755513724 553 YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 422-601 2.75e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 422 LKQKLEAKDIS-AVEEWKKKNEILAdrcgQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEM 500
Cdd:COG1196  218 LKEELKELEAElLLLKLRELEAELE----ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 501 RTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQ 580
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                        170       180
                 ....*....|....*....|.
gi 755513724 581 ISDLKRTISKLEAQVKQAEHE 601
Cdd:COG1196  374 LAEAEEELEELAEELLEALRA 394
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 450-601 5.45e-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: 51.85  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 450 QLDSALNEATSRVRTLEKnnnlleiEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAY 529
Cdd:COG1579   14 ELDSELDRLEHRLKELPA-------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755513724 530 KlsddkearlrqeNKMFQDLLGEYESLGKEhgrvkdtLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:COG1579   87 N------------NKEYEALQKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEAE 139
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 435-599 8.68e-07

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: 8.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   435 EEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRL 514
Cdd:TIGR02169  684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   515 KCRLQDLEEAFENAYKLSDDKEARLRQEnkMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQ 594
Cdd:TIGR02169  764 EARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841


                   ....*
gi 755513724   595 VKQAE 599
Cdd:TIGR02169  842 RIDLK 846
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 416-574 3.05e-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: 51.60  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   416 ESEISSLKQKLEaKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQE 495
Cdd:TIGR02168  781 EAEIEELEAQIE-QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755513724   496 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKL 574
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
418-604 4.04e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 418 EISSLKQKLEAKDiSAVEEWKKKNEILAdrcgQLDSALNEATSRVRTLEKNNNLLE--IEVSDLRERFNAASSASKVLQE 495
Cdd:COG4717   72 ELKELEEELKEAE-EKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPE 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 496 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQEnkmFQDLLGEYESLGKEHGRVKDTLNTTENKLL 575
Cdd:COG4717  147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELE 223

                        170       180
                 ....*....|....*....|....*....
gi 755513724 576 DAHTQISDLKRTISKLEAQVKQAEHESML 604
Cdd:COG4717  224 ELEEELEQLENELEAAALEERLKEARLLL 252
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 419-591 5.13e-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: 50.59  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  419 ISSLKQKLEAKDISAvEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIE 498
Cdd:pfam10174 326 IEVLKESLTAKEQRA-AILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  499 EMRTSNKEKDNTITRLKCRLQDLEE----------AFENAykLSdDKE---ARLR-QENKMFQDLLGEYESLGKEHGRVK 564
Cdd:pfam10174 405 NLQEQLRDKDKQLAGLKERVKSLQTdssntdtaltTLEEA--LS-EKEriiERLKeQREREDRERLEELESLKKENKDLK 481

                         170       180
                  ....*....|....*....|....*..
gi 755513724  565 DTLNTTENKLLDAHTQISDLKRTISKL 591
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSL 508
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
393-599 6.07e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 393 LSKIRQNLKE-----KHARHVADLRAYYEsEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLD---SALNEATSRVRT 464
Cdd:PRK03918 475 ERKLRKELRElekvlKKESELIKLKELAE-QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKLEE 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 465 LEKNNNLLEIEVSDLRERF--------NAASSASKVLQERIEEMR----------TSNKEKDNTITRLKCRLQDLEEAFE 526
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELaellkeleELGFESVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 527 NAYKLSDD---KEARLRQENKMFQD-----LLGEYESLGKEHGRVKDTLNTTENklldahtQISDLKRTISKLEAQVKQA 598
Cdd:PRK03918 634 ELAETEKRleeLRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEK-------RREEIKKTLEKLKEELEER 706


                 .
gi 755513724 599 E 599
Cdd:PRK03918 707 E 707
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 416-601 6.29e-06

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: 50.02  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  416 ESEISSLKQKLEAKDiSAVEEWKKKNEILADRCGQLDSALNEATS--------------RVRTLEKNNNLLEIEVSDLRE 481
Cdd:TIGR04523 355 ESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESkiqnqeklnqqkdeQIKKLQQEKELLEKEIERLKE 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  482 RFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLgkehg 561
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL----- 508

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 755513724  562 rvkdtlnttENKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:TIGR04523 509 ---------EEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
396-620 7.30e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 7.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 396 IRQNLKEKHARhVADLRAYYESEISSLKQKLEAKDiSAVEEWKKKNEI---------LADRCGQLDSALNEAT------- 459
Cdd:COG3206  162 LEQNLELRREE-ARKALEFLEEQLPELRKELEEAE-AALEEFRQKNGLvdlseeaklLLQQLSELESQLAEARaelaeae 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 460 SRVRTLEKNNNL-----------------------LEIEVSDLRERFNAASSASKVLQERIEEMRTS-NKEKDNTITRLK 515
Cdd:COG3206  240 ARLAALRAQLGSgpdalpellqspviqqlraqlaeLEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLE 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 516 CRLQDLEEAfENAYKlsdDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLldahtqisdlkrtiskLEAQV 595
Cdd:COG3206  320 AELEALQAR-EASLQ---AQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL----------------EEARL 379

                        250       260
                 ....*....|....*....|....*
gi 755513724 596 KQAEHESMLSLRNGAKVPERPSRSN 620
Cdd:COG3206  380 AEALTVGNVRVIDPAVVPLKPVSPK 404
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 415-601 7.82e-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: 50.06  E-value: 7.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   415 YESEISSLKQKLEAKD--ISAVEEwkkKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKV 492
Cdd:TIGR02168  244 LQEELKEAEEELEELTaeLQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   493 LQERIEemrtsnkEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTEN 572
Cdd:TIGR02168  321 LEAQLE-------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393

                          170       180
                   ....*....|....*....|....*....
gi 755513724   573 KLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQE 422
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 393-599 8.50e-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: 50.07  E-value: 8.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   393 LSKIRQNLKEKHARHVADLrAYYESEISSLKQKLEA-KDISAVEEWKKKN---EILADRCGQLDSALNEATSRVRTLEKN 468
Cdd:TIGR02169  749 LEQEIENVKSELKELEARI-EELEEDLHKLEEALNDlEARLSHSRIPEIQaelSKLEEEVSRIEARLREIEQKLNRLTLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   469 NNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEafenayKLSDDKEARLRQENKMfqd 548
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES------RLGDLKKERDELEAQL--- 898

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755513724   549 llgeyeslgkehGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 599
Cdd:TIGR02169  899 ------------RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
402-599 9.85e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 9.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 402 EKHARHVADLRAYYESEISSLKQKLEAKdiSAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRE 481
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRT--ENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELEE 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 482 RFnaassaskvlqERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMfQDLLGEYESLGKEHG 561
Cdd:PRK03918 236 LK-----------EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYE 303

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755513724 562 RVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 599
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 392-599 1.27e-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: 49.28  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   392 MLSKIRQNLKEKHARHVAdlrAYYESEISSLKQKLEAKDIS----AVEEWKKKNEILADRCGQLDSALNEA-------TS 460
Cdd:TIGR02168  713 ELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAqlskELTELEAEIEELEERLEEAEEELAEAeaeieelEA 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   461 RVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLR 540
Cdd:TIGR02168  790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 755513724   541 QENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 599
Cdd:TIGR02168  870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 397-597 2.04e-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: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   397 RQNLKEKHARHVADLRAYYESEISSLKQKLEaKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEV 476
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   477 SDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESL 556
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 755513724   557 GKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQ 597
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 409-599 2.30e-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: 47.84  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 409 ADLRAYYESEISSLKQKLEAKDISAVEEWKKKNEILADRcGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASS 488
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 489 ASKVLQERIEEM-----RTSN------------------------------KEKDNTITRLKCRLQDLEEAFENAYKLSD 533
Cdd:COG4942   98 ELEAQKEELAELlralyRLGRqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAERAELE 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755513724 534 DKEARLRQENKMFQDLLGEYESLGKehgRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 599
Cdd:COG4942  178 ALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
411-614 4.95e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 4.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 411 LRAYYES--EISSLKQKLEaKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASS 488
Cdd:PRK02224 243 LEEHEERreELETLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 489 ASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEE--------------AFENAYKLSDDKEARLRQENKMFQDLLGEYE 554
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreeaaelesELEEAREAVEDRREEIEELEEEIEELRERFG 401

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 555 SLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEhesmlSLRNGAKVPE 614
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE-----ALLEAGKCPE 456
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 392-659 6.90e-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: 46.98  E-value: 6.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   392 MLSKIRQNLkEKHARHVADLRAYyeSEISSLKQKLEAKDISAveEWKKKNEILADRCGQLDSA---LNEATSRVRTLEKN 468
Cdd:TIGR02169  192 IIDEKRQQL-ERLRREREKAERY--QALLKEKREYEGYELLK--EKEALERQKEAIERQLASLeeeLEKLTEEISELEKR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   469 NNLLEIEVSDLRERFNAASSASKV-LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQ 547
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   548 DLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHESMLSLRNGAKVPERPSRsnsvATSDV 627
Cdd:TIGR02169  347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR----LSEEL 422

                          250       260       270
                   ....*....|....*....|....*....|..
gi 755513724   628 SRRKWLIPGAEysiftGQPLDPRDRKLDKQLE 659
Cdd:TIGR02169  423 ADLNAAIAGIE-----AKINELEEEKEDKALE 449
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 393-601 1.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 393 LSKIRQNLKEKHARHVADLRAYyESEISSLKQKLEAKDIsAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLL 472
Cdd:COG1196  244 LEAELEELEAELEELEAELAEL-EAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 473 EIEVSDLRERFNAassaskvLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGE 552
Cdd:COG1196  322 EEELAELEEELEE-------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755513724 553 YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:COG1196  395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 444-599 1.16e-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: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 444 LADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMR------TSNKEKDN---TITRL 514
Cdd:COG1579   22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKEYEAlqkEIESL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 515 KCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEhgrvkdtlnttenklLDAhtQISDLKRTISKLEAQ 594
Cdd:COG1579  102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---------------LDE--ELAELEAELEELEAE 164


                 ....*
gi 755513724 595 VKQAE 599
Cdd:COG1579  165 REELA 169
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 393-556 1.50e-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: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 393 LSKIRQNLKEkHARHVADLrayyESEISSLKQKLEA--KDISAVEEWKKKNEILADrcgQLDSALNEATSRVRTLEKNNN 470
Cdd:COG1579   19 LDRLEHRLKE-LPAELAEL----EDELAALEARLEAakTELEDLEKEIKRLELEIE---EVEARIKKYEEQLGNVRNNKE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 471 L--LEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE-----N 543
Cdd:COG1579   91 YeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEreelaA 170

                        170
                 ....*....|...
gi 755513724 544 KMFQDLLGEYESL 556
Cdd:COG1579  171 KIPPELLALYERI 183
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 416-602 1.70e-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: 43.74  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  416 ESEISSLKQKLEakdisaveEWKKKNEILADRCGQLDSALNeatsrvRTLEKNNNLLEI------EVSDLRERFnaassa 489
Cdd:pfam15619  17 QNELAELQSKLE--------ELRKENRLLKRLQKRQEKALG------KYEGTESELPQLiarhneEVRVLRERL------ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  490 sKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEeafenayKLSDDK---------------EARLRQENKMFQDLLGEYE 554
Cdd:pfam15619  77 -RRLQEKERDLERKLKEKEAELLRLRDQLKRLE-------KLSEDKnlaereelqkkleqlEAKLEDKDEKIQDLERKLE 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755513724  555 SLGKEHGRvkdTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHES 602
Cdd:pfam15619 149 LENKSFRR---QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
475-601 2.10e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 475 EVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQEN-------KMFQ 547
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeelqEELE 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755513724 548 DLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:COG4372  119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
394-599 2.16e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 394 SKIRQNLKEKHARHVADLRAYyeSEISSLKQKLEAKdISAVEEWKKKNEILADRcgqldsaLNEATSRVRTLEKNNNLLE 473
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREI--NEISSELPELREE-LEKLEKEVKELEELKEE-------IEELEKELESLEGSKRKLE 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 474 IEVSDLRERFNAASSASKVLQERI----------EEMRTSNKEKDNT---ITRLKCRLQDLEEAFENAYKLSDD---KEA 537
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVkelkelkekaEEYIKLSEFYEEYldeLREIEKRLSRLEEEINGIEERIKEleeKEE 338

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755513724 538 RLRQENKMFQDLLGEYESLGKEHgRVKDTLNTTENKLLDAHTQISDLkrTISKLEAQVKQAE 599
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELE 397
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
408-597 3.32e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 408 VADLRAYYESEISSLKQK---LEAkDISAVEEWKKKNEILAD-----RCGQ--LDS----ALNEATSRVRTLEKNNNLLE 473
Cdd:PRK02224 410 AEDFLEELREERDELREReaeLEA-TLRTARERVEEAEALLEagkcpECGQpvEGSphveTIEEDRERVEELEAELEDLE 488

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 474 IEVSDLRERFNAASSASKV-------------LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAfenayklSDDKEARLR 540
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEAedrierleerredLEELIAERRETIEEKRERAEELRERAAELEAE-------AEEKREAAA 561

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755513724 541 QENKMFQDLLGEYESLGKEHGRVKDTLNTTeNKLLDAHTQISDLKRTISKLEAQVKQ 597
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREA 617
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 436-607 3.43e-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: 43.85  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   436 EWKKKneILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMrtsNKEKDNTITRLK 515
Cdd:smart00787 136 EWRMK--LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDEL---EDCDPTELDRAK 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   516 CRLQDLEEAFENAYKLSDDKEARLRQenkmfqdllgeyeslgkehgrVKDTLNTTENKLLDAHTQISDLKRT-------- 587
Cdd:smart00787 211 EKLKKLLQEIMIKVKKLEELEEELQE---------------------LESKIEDLTNKKSELNTEIAEAEKKleqcrgft 269

                          170       180
                   ....*....|....*....|...
gi 755513724   588 ---ISKLEAQVKQAEHESMLSLR 607
Cdd:smart00787 270 fkeIEKLKEQLKLLQSLTGWKIT 292
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
405-605 4.01e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 405 ARHVADLRAYYESEISSLKQKLEAKDISAVEEWKKkneiLADRCGQLDSALNEATSRVRTLEKNNnlLEIEVSDLRERFN 484
Cdd:COG4717  307 LQALPALEELEEEELEELLAALGLPPDLSPEELLE----LLDRIEELQELLREAEELEEELQLEE--LEQEIAALLAEAG 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 485 AASSASkvLQERIEEMRtsnkekdntitrlkcRLQDLEEAFENAyklsddkEARLRQENKMFQDLLgeyESLGKEhgRVK 564
Cdd:COG4717  381 VEDEEE--LRAALEQAE---------------EYQELKEELEEL-------EEQLEELLGELEELL---EALDEE--ELE 431

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755513724 565 DTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHESMLS 605
Cdd:COG4717  432 EELEELEEELEELEEELEELREELAELEAELEQLEEDGELA 472
Filament pfam00038
Intermediate filament protein;
461-542 4.52e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 43.37  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  461 RVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQER-IEEMRtsNKEKDNTITRLKCRLQ--DLEEAFENaYKLSDDKEA 537
Cdd:pfam00038  19 KVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKeIEDLR--RQLDTLTVERARLQLEldNLRLAAED-FRQKYEDEL 95


                  ....*
gi 755513724  538 RLRQE 542
Cdd:pfam00038  96 NLRTS 100
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 399-601 4.65e-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: 44.24  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  399 NLKEKHARHVADLRAYYESEISSLKQKLEAKDISaVEEWKKKNEILADrcgQLDSALNEATSRVRTLEKNNNLLEIEVSD 478
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI-IKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKE 497

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  479 LRERFNAASSAS---KVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFE--NAYKLSDDKEARLRQENKMFQDLLGEY 553
Cdd:TIGR04523 498 LKKLNEEKKELEekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQTQ 577

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755513724  554 ESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
408-598 4.83e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 408 VADLRAYYESEISSLKQKLEAKDISA-------------VEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEI 474
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAqahneeaeslredADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 475 EVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAyklsddkeARLRQENK---MFQDLLG 551
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA--------EALLEAGKcpeCGQPVEG 463

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755513724 552 EYESLGKEHGRVKdtLNTTENKLLDAHTQISDLKRTISKLEAQVKQA 598
Cdd:PRK02224 464 SPHVETIEEDRER--VEELEAELEDLEEEVEEVEERLERAEDLVEAE 508
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
434-608 6.83e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 434 VEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERfnaASSASKVLQERIEEMRTSNKEKDNTITR 513
Cdd:COG1340   10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE---AQELREKRDELNEKVKELKEERDELNEK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 514 LKCRLQDLEEAFENAYKLSDDK------EARLRQENKMFQ----------DLLGEYESLGKEHGRVKDtLNTTENKLLDA 577
Cdd:COG1340   87 LNELREELDELRKELAELNKAGgsidklRKEIERLEWRQQtevlspeeekELVEKIKELEKELEKAKK-ALEKNEKLKEL 165

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755513724 578 HTQISDLKRTISKLEAQVK------QAEHESMLSLRN 608
Cdd:COG1340  166 RAELKELRKEAEEIHKKIKelaeeaQELHEEMIELYK 202
PRK09039 PRK09039
peptidoglycan -binding protein;
452-586 8.39e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 8.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 452 DSALNEATSRVR------TLEKNNNL-LEIEVSDLRERFNAASSaskvLQERIEEMRTsnkEKDNTITRLKCRLQDLEEA 524
Cdd:PRK09039  52 DSALDRLNSQIAeladllSLERQGNQdLQDSVANLRASLSAAEA----ERSRLQALLA---ELAGAGAAAEGRAGELAQE 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755513724 525 FENAYKLSDDKEARLrqenkmfqDLLGE-YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKR 586
Cdd:PRK09039 125 LDSEKQVSARALAQV--------ELLNQqIAALRRQLAALEAALDASEKRDRESQAKIADLGR 179
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
409-580 1.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  409 ADLRAYYESEISSLKQKLEA--KDISAVEEWKKKNEILADRCGQLDsALNEATSRVRTLEKnnnllEI-EVSDLRERFNA 485
Cdd:COG4913   609 RAKLAALEAELAELEEELAEaeERLEALEAELDALQERREALQRLA-EYSWDEIDVASAER-----EIaELEAELERLDA 682

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  486 ASSASKVLQERIE----EMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE-----NKMFQDLLGE- 552
Cdd:COG4913   683 SSDDLAALEEQLEeleaELEELEEELDelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElrallEERFAAALGDa 762

                         170       180       190
                  ....*....|....*....|....*....|...
gi 755513724  553 -----YESLGKEHGRVKDTLNTTENKLLDAHTQ 580
Cdd:COG4913   763 verelRENLEERIDALRARLNRAEEELERAMRA 795
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 493-601 1.38e-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: 42.74  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   493 LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMF-------QDLLGEYESLGKEHGRVKD 565
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaevEQLEERIAQLSKELTELEA 761

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 755513724   566 TLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 383-599 1.40e-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: 42.65  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   383 SLASLEDPVMLSKIRQNlKEKHARHVADLRAYYESEISSLKQKLEAKDISAVEEWKKKNEILadrcgqldsalNEATSRV 462
Cdd:TIGR00618  664 ALSIRVLPKELLASRQL-ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE-----------NASSSLG 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724   463 RTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE 542
Cdd:TIGR00618  732 SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 755513724   543 NKMFQD-LLGEYESLGKEhgrvkdtLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 599
Cdd:TIGR00618  812 IPSDEDiLNLQCETLVQE-------EEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
393-553 1.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 393 LSKIRQNLKEKHARHVADLrayyESEISSL----KQKLEAKDI-SAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEK 467
Cdd:PRK03918 572 LAELLKELEELGFESVEEL----EERLKELepfyNEYLELKDAeKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 468 NNNLLEIEVSD-----LRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKE--ARLR 540
Cdd:PRK03918 648 ELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALErvEELR 727

                        170
                 ....*....|...
gi 755513724 541 QENKMFQDLLGEY 553
Cdd:PRK03918 728 EKVKKYKALLKER 740
46 PHA02562
endonuclease subunit; Provisional
 418-601 2.68e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 418 EISSLKQKLEAKDISAVEEWKKKNEILADRCGQLDSALNEAtsrvRTLEKNNNLLEIEVSDL-RERFNAASSASKVLQER 496
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA----KTIKAEIEELTDELLNLvMDIEDPSAALNKLNTAA 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 497 IE---EMRTSNKE----KDNTItrlkCR--LQDLEEAFENAYKLSDdKEARLRQENKMFQDLLGEYESLgkehgrvKDTL 567
Cdd:PHA02562 265 AKiksKIEQFQKVikmyEKGGV----CPtcTQQISEGPDRITKIKD-KLKELQHSLEKLDTAIDELEEI-------MDEF 332

                        170       180       190
                 ....*....|....*....|....*....|....
gi 755513724 568 NTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAA 366
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 398-615 2.74e-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: 41.42  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  398 QNLKEKHARHVADL-RAYYESEISSLKQKLEAKdiSAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEV 476
Cdd:pfam07888  33 QNRLEECLQERAELlQAQEAANRQREKEKERYK--RDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  477 SDLRERFNAASSASKVLQERIEEMRTSNK-------EKDNTITRLKCRLQDL------EEAFENAYKLS-DDKEARLRQE 542
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKtltqrvlERETELERMKERAKKAgaqrkeEEAERKQLQAKlQQTEEELRSL 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755513724  543 NKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLkrtiskleaqvkQAEHESMLSLRNGAKVPER 615
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN------------EALLEELRSLQERLNASER 251
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 416-601 3.08e-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: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 416 ESEISSLKQKLEAKDISAVEEwKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQE 495
Cdd:COG1196  301 EQDIARLEERRRELEERLEEL-EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 496 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAyklsDDKEARLRQENKMFQD----LLGEYESLGKEHGRVKDTLNTTE 571
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEAL----LERLERLEEELEELEEalaeLEEEEEEEEEALEEAAEEEAELE 455

                        170       180       190
                 ....*....|....*....|....*....|
gi 755513724 572 NKLLDAHTQISDLKRTISKLEAQVKQAEHE 601
Cdd:COG1196  456 EEEEALLELLAELLEEAALLEAALAELLEE 485
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
368-503 3.85e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 368 QSQLPGTANSVPECIS----------LASLEdpVMLSKIRQNLKEKHARhVADLRAyyesEISSLKQKLEAKDISAVEEW 437
Cdd:COG3206  246 RAQLGSGPDALPELLQspviqqlraqLAELE--AELAELSARYTPNHPD-VIALRA----QIAALRAQLQQEAQRILASL 318

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755513724 438 KKKNEILADRCGQLDSALNEATSRVRTLeknnNLLEIEVSDLRERFNAASSASKVLQERIEEMRTS 503
Cdd:COG3206  319 EAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLEEARLA 380
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 384-577 3.95e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 39.74  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 384 LASLEDPVMLSKIrQNLKEKHARHVADLRAYYE--SEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLdsaLNEATSR 461
Cdd:cd00176   23 LSSTDYGDDLESV-EALLKKHEALEAELAAHEErvEALNELGEQLIEEGHPDAEEIQERLEELNQRWEEL---RELAEER 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 462 VRTLEknnnlleiEVSDLRERFNAASSASKVLQERIEEMRTSNKEKD-NTITRLKCRLQDLEEAFENayklsddKEARLR 540
Cdd:cd00176   99 RQRLE--------EALDLQQFFRDADDLEQWLEEKEAALASEDLGKDlESVEELLKKHKELEEELEA-------HEPRLK 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755513724 541 QENKMFQDLLGEYESLGKEHGRVK-DTLNTTENKLLDA 577
Cdd:cd00176  164 SLNELAEELLEEGHPDADEEIEEKlEELNERWEELLEL 201
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
409-594 5.46e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 409 ADLRAY--YESEISSLKQKLEAK-DISAVeewkkKNEILAdrcGQ-LDSALNEATSRVRTLEKNNNLL-----EIEVSDL 479
Cdd:COG2433  340 AALKAYdaYKNKFERVEKKVPPDvDRDEV-----KARVIR---GLsIEEALEELIEKELPEEEPEAERekeheERELTEE 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 480 RERFnaassasKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEafenayKLsddKEARLRQENKMFQDllGEYESLGKE 559
Cdd:COG2433  412 EEEI-------RRLEEQVERLEAEVEELEAELEEKDERIERLER------EL---SEARSEERREIRKD--REISRLDRE 473

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755513724 560 HGRVKDTLNTTENKLLDAHTQISDLKRTIsKLEAQ 594
Cdd:COG2433  474 IERLERELEEERERIEELKRKLERLKELW-KLEHS 507
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
 498-649 5.63e-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: 40.17  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  498 EEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKL-SDDKEARLRQENKMFQDllgeyESLGKEHGRvKDTLNTTENKLLD 576
Cdd:TIGR00570 120 KKIETYQKENKDVIQKNKEKSTREQEELEEALEFeKEEEEQRRLLLQKEEEE-----QQMNKRKNK-QALLDELETSTLP 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755513724  577 AHTQISDLKRTISKLEAQVKQAEHESMLSLRNGAKVPERPSRSNsvatsdvsrrkwlIPGAEYSIFTGQPLDP 649
Cdd:TIGR00570 194 AAELIAQHKKNSVKLEMQVEKPKPEKPNTFSTGIKMGYQISLVP-------------VQKSEEALYPYQPLNI 253
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
444-608 6.65e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 444 LADRCGQLDSALNEATSRVR-----TLEKNNNLLEIEVSD---------------------LRERFNAASSASKVLQERI 497
Cdd:COG3206  105 LDEDPLGEEASREAAIERLRknltvEPVKGSNVIEISYTSpdpelaaavanalaeayleqnLELRREEARKALEFLEEQL 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 498 EEMRTSNKEKDNTIT--RLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTtenklL 575
Cdd:COG3206  185 PELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE-----L 259

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755513724 576 DAHTQISDLKRTISKLEAQVKQ------AEHESMLSLRN 608
Cdd:COG3206  260 LQSPVIQQLRAQLAELEAELAElsarytPNHPDVIALRA 298
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 400-612 7.09e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  400 LKEKHARhVADLRAYYESEISSLKQKLEAKDISAVEEWKKKNEiladrcgqLDSALNEATSRVRTLEKNNNLLEIEVSDL 479
Cdd:pfam05483 217 LKEDHEK-IQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKD--------LTFLLEESRDKANQLEEKTKLQDENLKEL 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724  480 RERFNAassaskvLQERIEEMRTSNKEKDNTITRLKcrlQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKE 559
Cdd:pfam05483 288 IEKKDH-------LTKELEDIKMSLQRSMSTQKALE---EDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755513724  560 HGRVKDTLNTTENKLLDAHTQISdlkrtISKLEAQVKQAEHESMLSLRNGAKV 612
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLK-----IITMELQKKSSELEEMTKFKNNKEV 405
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
447-599 7.84e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 7.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 447 RCGQLDSALNEATSRVRTLEK----------NNNLLEI--EVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRL 514
Cdd:PRK03918 133 RQGEIDAILESDESREKVVRQilglddyenaYKNLGEVikEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513724 515 KCRLQDLEEAFENayklsddkearLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQ 594
Cdd:PRK03918 213 SSELPELREELEK-----------LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281


                 ....*
gi 755513724 595 VKQAE 599
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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