NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767942806|ref|XP_011534112|]
View 

centrosomal protein of 85 kDa-like isoform X2 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 374-633 1.47e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   374 LRQKEIVIdrQKQQITHLHERIRdnELRAQHAMLGHYVNCEDSYVASLQLK--TRDRYISSLKKKCQKESEQNKEKQRRI 451
Cdd:TIGR02168  222 LRELELAL--LVLRLEELREELE--ELQEELKEAEEELEELTAELQELEEKleELRLEVSELEEEIEELQKELYALANEI 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   452 ETLEKYL----ADLPTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSL 526
Cdd:TIGR02168  298 SRLEQQKqilrERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   527 QQKVERcLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EEL 601
Cdd:TIGR02168  378 EEQLET-LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEEL 456

                          250       260       270
                   ....*....|....*....|....*....|..
gi 767942806   602 EKKERNVQRLTKALLENQRQTDETCSLLDQGQ 633
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQLQ 488
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 374-633 1.47e-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: 58.53  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   374 LRQKEIVIdrQKQQITHLHERIRdnELRAQHAMLGHYVNCEDSYVASLQLK--TRDRYISSLKKKCQKESEQNKEKQRRI 451
Cdd:TIGR02168  222 LRELELAL--LVLRLEELREELE--ELQEELKEAEEELEELTAELQELEEKleELRLEVSELEEEIEELQKELYALANEI 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   452 ETLEKYL----ADLPTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSL 526
Cdd:TIGR02168  298 SRLEQQKqilrERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   527 QQKVERcLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EEL 601
Cdd:TIGR02168  378 EEQLET-LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEEL 456

                          250       260       270
                   ....*....|....*....|....*....|..
gi 767942806   602 EKKERNVQRLTKALLENQRQTDETCSLLDQGQ 633
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 443-641 1.93e-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: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 443 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTT 522
Cdd:COG1196  219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 523 VQSLQQKVERCLEDGIRLPmLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELE 602
Cdd:COG1196  297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767942806 603 KKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQ 641
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
421-606 6.48e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 421 LQLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQL-----QILEEKNkNLQEALIDTEKKL 495
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLsefyeEYLDELR-EIEKRLSRLEEEI 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 496 EEIKKQCQDKETqlicQKKKEKELVTTVQSLQQKVERcLEDGIRLpMLDAKQLQNENDNLRQQ--NETASKI------ID 567
Cdd:PRK03918 324 NGIEERIKELEE----KEERLEELKKKLKELEKRLEE-LEERHEL-YEEAKAKKEELERLKKRltGLTPEKLekeleeLE 397

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767942806 568 SQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKER 606
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 431-639 3.36e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.96  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  431 SSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvQSQSLQLQIleEKNKNLQEALIDTEKKLEEIKKQCQDKETQLI 510
Cdd:pfam05557  37 SALKRQLDRESDRNQELQKRIRLLEKREAE-------AEEALREQA--ELNRLKKKYLEALNKKLNEKESQLADAREVIS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  511 CQKKKEKELVT-------TVQSLQQKVERCLEdgiRLPMLDAKqLQNENDnLRQQNETASKIIDSQQDEIDRMILEIQSM 583
Cdd:pfam05557 108 CLKNELSELRRqiqraelELQSTNSELEELQE---RLDLLKAK-ASEAEQ-LRQNLEKQQSSLAEAEQRIKELEFEIQSQ 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767942806  584 qgklSKEKLTTQKMMEELE---KKERNVQRLtKALLENQRQTDETCSLLDQGQEPDQSR 639
Cdd:pfam05557 183 ----EQDSEIVKNSKSELAripELEKELERL-REHNKHLNENIENKLLLKEEVEDLKRK 236
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 544-631 2.90e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   544 DAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTT-----QKMMEELEKKERNVQRLTKALLE- 617
Cdd:smart00935   5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLseaarEKKEKELQKKVQEFQRKQQKLQQd 84

                           90
                   ....*....|....*
gi 767942806   618 -NQRQTDETCSLLDQ 631
Cdd:smart00935  85 lQKRQQEELQKILDK 99
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 374-633 1.47e-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: 58.53  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   374 LRQKEIVIdrQKQQITHLHERIRdnELRAQHAMLGHYVNCEDSYVASLQLK--TRDRYISSLKKKCQKESEQNKEKQRRI 451
Cdd:TIGR02168  222 LRELELAL--LVLRLEELREELE--ELQEELKEAEEELEELTAELQELEEKleELRLEVSELEEEIEELQKELYALANEI 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   452 ETLEKYL----ADLPTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSL 526
Cdd:TIGR02168  298 SRLEQQKqilrERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   527 QQKVERcLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EEL 601
Cdd:TIGR02168  378 EEQLET-LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEEL 456

                          250       260       270
                   ....*....|....*....|....*....|..
gi 767942806   602 EKKERNVQRLTKALLENQRQTDETCSLLDQGQ 633
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 443-641 1.93e-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: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 443 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTT 522
Cdd:COG1196  219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 523 VQSLQQKVERCLEDGIRLPmLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELE 602
Cdd:COG1196  297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767942806 603 KKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQ 641
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 374-649 2.88e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 374 LRQKEIVIDRQKQQITHLHERIRDNELRAQHAMLGHYVNCEDSYVASLQLKTRDRYISSLKKKCQKESEQNKEKQRRIET 453
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 454 LEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEikkqcqdketqlicQKKKEKELVTTVQSLQQKVERC 533
Cdd:COG1196  321 LEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAE--------------AEEALLEAEAELAEAEEELEEL 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 534 LEDGIRLpMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTK 613
Cdd:COG1196  385 AEELLEA-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767942806 614 ALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPL 649
Cdd:COG1196  464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
421-606 6.48e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 421 LQLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQL-----QILEEKNkNLQEALIDTEKKL 495
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLsefyeEYLDELR-EIEKRLSRLEEEI 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 496 EEIKKQCQDKETqlicQKKKEKELVTTVQSLQQKVERcLEDGIRLpMLDAKQLQNENDNLRQQ--NETASKI------ID 567
Cdd:PRK03918 324 NGIEERIKELEE----KEERLEELKKKLKELEKRLEE-LEERHEL-YEEAKAKKEELERLKKRltGLTPEKLekeleeLE 397

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767942806 568 SQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKER 606
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 443-641 1.67e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 443 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqKKKEKELVTT 522
Cdd:COG3883   17 QIQAKQKELSELQAELEAA--QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGER 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 523 VQSLQQkvercleDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDrmilEIQSMQGKLSKEKLTTQKMMEELE 602
Cdd:COG3883   92 ARALYR-------SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELE 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767942806 603 KKERNVQRLTKALlenQRQTDETCSLLDQGQEPDQSRQQ 641
Cdd:COG3883  161 ALKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEA 196
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 364-625 1.97e-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: 51.17  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  364 ESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNElraqhamlghyvncEDSYVASLQLKTRDRYISSLKKKCQKESEQ 443
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT--------------NQDSVKELIIKNLDNTRESLETQLKVLSRS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  444 NKEKQRRIETLEKYLA----DLPTLDDVQSQslqlqiLEEKNKNL---QEALIDTEKKLE----EIKKQCQDKETQLICQ 512
Cdd:TIGR04523 477 INKIKQNLEQKQKELKskekELKKLNEEKKE------LEEKVKDLtkkISSLKEKIEKLEsekkEKESKISDLEDELNKD 550

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  513 K--KKEKELVTTVQSLQQKVErcledgirlpmldakQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQ---SMQGKL 587
Cdd:TIGR04523 551 DfeLKKENLEKEIDEKNKEIE---------------ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEekeKKISSL 615

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767942806  588 SKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDET 625
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 358-624 2.63e-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: 50.79  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  358 QDFSKW-ESMLKIKEGLLRQKEIVIDRQKQQITHLHERI----------------RDNELRAQHAMLGHYVNCEDSYVAS 420
Cdd:TIGR04523 306 QDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQIsqlkkeltnsesenseKQRELEEKQNEIEKLKKENQSYKQE 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  421 LQ-LKTRdryISSLKKKCQKESEQNKEKQRRIETLEKYLADLptldDVQSQSLQLQILEEKN--KNLQEALIDTEKKLEE 497
Cdd:TIGR04523 386 IKnLESQ---INDLESKIQNQEKLNQQKDEQIKKLQQEKELL----EKEIERLKETIIKNNSeiKDLTNQDSVKELIIKN 458

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  498 IKKQCQDKETQLicqKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETASKIIDSQQDEIDR 575
Cdd:TIGR04523 459 LDNTRESLETQL---KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEekKELEEKVKDLTKKISSLKEKIEKLESEKKE 535

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767942806  576 MILEIQSMQGKLSKEK--LTTQKMMEELEKKERNVQRL---TKALLENQRQTDE 624
Cdd:TIGR04523 536 KESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQE 589
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 358-611 3.72e-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: 50.45  E-value: 3.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   358 QDFSKWESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAqhamlghyvNCEDSYVASLQLKTRDRYISSLKKKC 437
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL---------HKLEEALNDLEARLSHSRIPEIQAEL 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   438 QKESEQNKEKQRRIETLEKYLadlptlddvQSQSLQLQILEEKNKNLQEALIDTE-------KKLEEIKKQCQDKETQLI 510
Cdd:TIGR02169  801 SKLEEEVSRIEARLREIEQKL---------NRLTLEKEYLEKEIQELQEQRIDLKeqiksieKEIENLNGKKEELEEELE 871

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   511 CQKKKEKELVTTVQSLQQKVERCLEDG----IRLPMLDAkQLQNENDNLRQQNETASkIIDSQQDEIDRMILEIQSMqgk 586
Cdd:TIGR02169  872 ELEAALRDLESRLGDLKKERDELEAQLreleRKIEELEA-QIEKKRKRLSELKAKLE-ALEEELSEIEDPKGEDEEI--- 946

                          250       260
                   ....*....|....*....|....*
gi 767942806   587 lSKEKLTTQKMMEELEKKERNVQRL 611
Cdd:TIGR02169  947 -PEEELSLEDVQAELQRVEEEIRAL 970
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 422-639 4.31e-06

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: 49.76  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 422 QLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKyladlptlddvqsqslQLQILEEKNKNLQEALIDTEKKLEEIKKQ 501
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALER----------------RIAALARRIRALEQELAALEAELAELEKE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 502 CQDKETQLICQKKKEKELVTTVQSLQQ--------KVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETASKI---IDS 568
Cdd:COG4942   92 IAELRAELEAQKEELAELLRALYRLGRqpplalllSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALraeLEA 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767942806 569 QQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSR 639
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 485-647 4.87e-06

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: 49.38  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 485 QEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRLPMLDAKQLQNENDNLRQQNETASK 564
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 565 IIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKA---LLENQRQTDETCSLLDQGQEPDQSRQQ 641
Cdd:COG4942   98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELE 177


                 ....*.
gi 767942806 642 TVLSKR 647
Cdd:COG4942  178 ALLAEL 183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 364-608 9.64e-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: 49.30  E-value: 9.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   364 ESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAQhaMLGHYVNCEDSYVASL--QLKTRDRYISSLKKKCQKES 441
Cdd:TIGR02169  790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEIQELQEQRIDLkeQIKSIEKEIENLNGKKEELE 867

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   442 EQNKEKQRRIETLEKYLADLptlddvqsqslqlqilEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVT 521
Cdd:TIGR02169  868 EELEELEAALRDLESRLGDL----------------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   522 TVQSLQQKVERCLEDGIRLPMLD--AKQLQNENDNLRQQNETASKIIDSQQDEIDRMiLEIQSMQGKLSKEKLTTQKMME 599
Cdd:TIGR02169  932 ELSEIEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIE 1010


                   ....*....
gi 767942806   600 ELEKKERNV 608
Cdd:TIGR02169 1011 EYEKKKREV 1019
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 367-617 1.89e-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: 48.13  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   367 LKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAQHAmlghyvncedsyvaSLQLKTRDRYISSLKKKCQKESEQNKE 446
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------------SRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   447 KQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSL 526
Cdd:TIGR02168  752 LSKELTELEAEIEEL--EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   527 QQKVERCLEdgirlpmlDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQ-------SMQGKLSKEKLTTQKMME 599
Cdd:TIGR02168  830 ERRIAATER--------RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEELSE 901

                          250
                   ....*....|....*...
gi 767942806   600 ELEKKERNVQRLTKALLE 617
Cdd:TIGR02168  902 ELRELESKRSELRRELEE 919
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
431-629 2.94e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 431 SSLKKKCQKESEQNKEKQRRIETLekylaDLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKEtQLI 510
Cdd:COG4717   45 AMLLERLEKEADELFKPQGRKPEL-----NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR-EEL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 511 CQKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDAK-----QLQNENDNLRQQNETASKIID--------SQQDEIDRMI 577
Cdd:COG4717  119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERleelrELEEELEELEAELAELQEELEelleqlslATEEELQDLA 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767942806 578 LEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALL--ENQRQTDETCSLL 629
Cdd:COG4717  199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEaaALEERLKEARLLL 252
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 459-647 6.88e-05

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: 44.92  E-value: 6.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 459 ADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcledgi 538
Cdd:COG1579    4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK------ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 539 rlpmldakqlqnenDNLRQQNETASKIIDSQQDEIDRMILEIQsmqgKLSKEKLttqKMMEELEKKERNVQRLTKALLEN 618
Cdd:COG1579   78 --------------YEEQLGNVRNNKEYEALQKEIESLKRRIS----DLEDEIL---ELMERIEELEEELAELEAELAEL 136

                        170       180
                 ....*....|....*....|....*....
gi 767942806 619 QRQTDETCSLLDQGQEPDQSRQQTVLSKR 647
Cdd:COG1579  137 EAELEEKKAELDEELAELEAELEELEAER 165
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
445-624 7.02e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 445 KEKQRRIETLEKYLADLPTLDD-VQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQ--DKETQLICQKKKEKELVT 521
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEElIKEKEKELEEVLREINEISSELPELREELEKLEKEVKelEELKEEIEELEKELESLE 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 522 -TVQSLQQKVeRCLEDGIRLPMLDAKQLQNENDNLRQQNETASK--IIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM 598
Cdd:PRK03918 252 gSKRKLEEKI-RELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330

                        170       180
                 ....*....|....*....|....*.
gi 767942806 599 EELEKKERNVQRLTKALLENQRQTDE 624
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEE 356
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 430-641 1.39e-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: 45.40  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  430 ISSLKKKCQKeseqNKEKQRRIETLEKYLADLPtlDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 509
Cdd:TIGR04523 203 LSNLKKKIQK----NKSLESQISELKKQNNQLK--DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  510 ICQKKKEKELVTTVQSLQQKVERcledgirlpmLDAKQLQNENDNLR---QQNETASKIIDSQQDEIDRMILEIQSMQGK 586
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISD----------LNNQKEQDWNKELKselKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767942806  587 LSKEK----LTTQKMMEELEKKERNVQRLTKallENQRQTDETCSLLDQGQEPDQSRQQ 641
Cdd:TIGR04523 347 LKKELtnseSENSEKQRELEEKQNEIEKLKK---ENQSYKQEIKNLESQINDLESKIQN 402
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 378-605 1.43e-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: 45.44  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   378 EIVIDRQKQQITHLhERIRDNELRAQhamlghyvncedsyvaSLQLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKY 457
Cdd:TIGR02169  190 DLIIDEKRQQLERL-RREREKAERYQ----------------ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   458 LADLPTLddvqsqslqlqiLEEKNKNLQEAlidtEKKLEEIKKQCQDKETQLICQKKKEkelvttVQSLQQKVERClEDG 537
Cdd:TIGR02169  253 LEKLTEE------------ISELEKRLEEI----EQLLEELNKKIKDLGEEEQLRVKEK------IGELEAEIASL-ERS 309

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767942806   538 IRLPMLDAKQLQNEndnlRQQNETaskiidsqqdEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKE 605
Cdd:TIGR02169  310 IAEKERELEDAEER----LAKLEA----------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
423-621 1.44e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 423 LKTRDRYISSLKKKCQKESE-----QNKEKQ-----RRIETLEKYLADLPT-LDDVQSQSLQLQILEEKNKNLQEALIDT 491
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENieeliKEKEKEleevlREINEISSELPELREeLEKLEKEVKELEELKEEIEELEKELESL 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 492 EKKLEEIKKQCQDKETQLICQKKKEKEL---VTTVQSLQQKVERCLEDGirlpmldaKQLQNENDNLRQQNETASKIiDS 568
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELeekVKELKELKEKAEEYIKLS--------EFYEEYLDELREIEKRLSRL-EE 321

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767942806 569 QQDEIDRMILEIQSMQ---GKLSKEKLTTQKMMEELEKKERNVQRLtKALLENQRQ 621
Cdd:PRK03918 322 EINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEA-KAKKEELER 376
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
424-593 1.54e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 424 KTRDRYISSLKKKCQKESEQnKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQ 503
Cdd:COG4717   85 EKEEEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 504 DKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRlpmlDAKQLQNENDNLRQQNETASKIIDSQQDEIDRM--ILEIQ 581
Cdd:COG4717  164 ELEELEAELAELQEELEELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELEEAQEELEELEEELEQLenELEAA 239

                        170
                 ....*....|..
gi 767942806 582 SMQGKLSKEKLT 593
Cdd:COG4717  240 ALEERLKEARLL 251
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 441-642 1.78e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 441 SEQNKEKQRRIETLEKyladlptldDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELV 520
Cdd:COG4942   19 ADAAAEAEAELEQLQQ---------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 521 TTVQSLQQKVERCLEDGIRlpMLDAKQLQNENDNLR--------QQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKL 592
Cdd:COG4942   90 KEIAELRAELEAQKEELAE--LLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767942806 593 TTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQT 642
Cdd:COG4942  168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 364-615 2.00e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   364 ESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAQHAmlghyvncedsyvaSLQLKTRDRYISSLKKKCQKESEQ 443
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL--------------SKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   444 NKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTV 523
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQL--KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   524 QSLQQKVERC--------------------LEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMIL----- 578
Cdd:TIGR02168  855 ESLAAEIEELeelieeleseleallnerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELrlegl 934

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 767942806   579 --EIQSMQGKLSKEKLTTQKMMEELEKK--------ERNVQRLTKAL 615
Cdd:TIGR02168  935 evRIDNLQERLSEEYSLTLEEAEALENKieddeeeaRRRLKRLENKI 981
PRK11281 PRK11281
mechanosensitive channel MscK;
421-661 2.52e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  421 LQLKTRDRY---ISSLKKKCQKESEQNKEKQRRIETLEKYLADlPTLDDVQSQSLqlqileeknKNLQEALIDTEKKLEE 497
Cdd:PRK11281   70 ALLDKIDRQkeeTEQLKQQLAQAPAKLRQAQAELEALKDDNDE-ETRETLSTLSL---------RQLESRLAQTLDQLQN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  498 IKKQCQDKETQLICQK----KKEKELVTTVQSLQQ--------KVERCLEDGIRLPMLDAKQ--LQNENDNLRQQNETAS 563
Cdd:PRK11281  140 AQNDLAEYNSQLVSLQtqpeRAQAALYANSQRLQQirnllkggKVGGKALRPSQRVLLQAEQalLNAQNDLQRKSLEGNT 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  564 KIID---SQQDE----IDRMILEIQSMQGKLSKEKLT-TQKMMEELEKKERNVQRLTKALL--ENQRQTDETCSLLDQGQ 633
Cdd:PRK11281  220 QLQDllqKQRDYltarIQRLEHQLQLLQEAINSKRLTlSEKTVQEAQSQDEAARIQANPLVaqELEINLQLSQRLLKATE 299

                         250       260
                  ....*....|....*....|....*...
gi 767942806  634 EPDQSRQQTVLSKRPLFDLTVIDQLFKE 661
Cdd:PRK11281  300 KLNTLTQQNLRVKNWLDRLTQSERNIKE 327
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 431-639 3.36e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.96  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  431 SSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvQSQSLQLQIleEKNKNLQEALIDTEKKLEEIKKQCQDKETQLI 510
Cdd:pfam05557  37 SALKRQLDRESDRNQELQKRIRLLEKREAE-------AEEALREQA--ELNRLKKKYLEALNKKLNEKESQLADAREVIS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  511 CQKKKEKELVT-------TVQSLQQKVERCLEdgiRLPMLDAKqLQNENDnLRQQNETASKIIDSQQDEIDRMILEIQSM 583
Cdd:pfam05557 108 CLKNELSELRRqiqraelELQSTNSELEELQE---RLDLLKAK-ASEAEQ-LRQNLEKQQSSLAEAEQRIKELEFEIQSQ 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767942806  584 qgklSKEKLTTQKMMEELE---KKERNVQRLtKALLENQRQTDETCSLLDQGQEPDQSR 639
Cdd:pfam05557 183 ----EQDSEIVKNSKSELAripELEKELERL-REHNKHLNENIENKLLLKEEVEDLKRK 236
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
367-517 4.37e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 367 LKIKEGLLRQKEIVIDRQKQQITHLHERIrdNELRAQHAMLGHYVNCEDSYVASLQLKTRDRYISSLKKKCQKESEQNKE 446
Cdd:COG4717   83 AEEKEEEYAELQEELEELEEELEELEAEL--EELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 447 KQRRIETLEKYLADL-------------PTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQK 513
Cdd:COG4717  161 LEEELEELEAELAELqeeleelleqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240


                 ....
gi 767942806 514 KKEK 517
Cdd:COG4717  241 LEER 244
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 303-584 6.12e-04

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 43.09  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  303 LTEQLRTNPLEGrntEDSYSLAPWQQQQIED----FRQGSETPmQVLTGSSRQSYSPGYQdFSKWESMLKIKEGLLRQKE 378
Cdd:pfam05667 252 IAEQLRSAALAG---TEATSGASRSAQDLAEllssFSGSSTTD-TGLTKGSRFTHTEKLQ-FTNEAPAATSSPPTKVETE 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  379 IviDRQKQQ---ITHLHERIRDNELRAQHAmlghyvncedsyvaSLQLKTRDRYISSLKKKCQKESEQNKEKQRRIETLE 455
Cdd:pfam05667 327 E--ELQQQReeeLEELQEQLEDLESSIQEL--------------EKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKK 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  456 KYLADLPTLD--------DVQSQSLQLQILEEKNKNLQEALIdteKKLEEIKKQCQDKETQliCQKKKEKelvttVQSLQ 527
Cdd:pfam05667 391 KTLDLLPDAEeniaklqaLVDASAQRLVELAGQWEKHRVPLI---EEYRALKEAKSNKEDE--SQRKLEE-----IKELR 460

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767942806  528 QKVERCLEDgIRLPMLDAKQLQNENDNLRQQ---NETASKI------IDSQQDEIDRMILEIQSMQ 584
Cdd:pfam05667 461 EKIKEVAEE-AKQKEELYKQLVAEYERLPKDvsrSAYTRRIleivknIKKQKEEITKILSDTKSLQ 525
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
422-592 8.09e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 8.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 422 QLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQ 501
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 502 cqdkETQLICQKKKEKELVTTVQSLQQKVERCLEDgIRLPMLDA-KQLQNENDNLRQQNETASKIIDSQQDEIDRMILEI 580
Cdd:COG4717  155 ----LEELRELEEELEELEAELAELQEELEELLEQ-LSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                        170
                 ....*....|..
gi 767942806 581 QSMQGKLSKEKL 592
Cdd:COG4717  230 EQLENELEAAAL 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 430-532 9.07e-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: 41.45  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 430 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 509
Cdd:COG1579   54 LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133

                         90       100
                 ....*....|....*....|...
gi 767942806 510 icqKKKEKELVTTVQSLQQKVER 532
Cdd:COG1579  134 ---AELEAELEEKKAELDEELAE 153
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 422-613 1.12e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 40.81  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  422 QLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQI---LEEKNKNLQEaLIDTEKKLEEI 498
Cdd:pfam05010  16 EIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIqkvLEEKDQALAD-LNSVEKSFSDL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  499 KKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcleDGIRLPMLDAKQLQNendnLRQQNETASKIIDSQQDEIdrmil 578
Cdd:pfam05010  95 FKRYEKQKEVISGYKKNEESLKKCAQDYLARIKK---EEQRYQALKAHAEEK----LDQANEEIAQVRSKAKAET----- 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767942806  579 eiQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTK 613
Cdd:pfam05010 163 --AALQASLRKEQMKVQSLERQLEQKTKENEELTK 195
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 422-591 1.26e-03

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: 40.66  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  422 QLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLddVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQ 501
Cdd:pfam15619  19 ELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQL--IARHNEEVRVLRERLRRLQEKERDLERKLKEKEAE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  502 CQDKETQLicqKKKEK-----------ELVTTVQSLQQKVERCLEDGIRLpmldAKQLQNENDNLRQQNETASKIIDSQQ 570
Cdd:pfam15619  97 LLRLRDQL---KRLEKlsedknlaereELQKKLEQLEAKLEDKDEKIQDL----ERKLELENKSFRRQLAAEKKKHKEAQ 169

                         170       180
                  ....*....|....*....|.
gi 767942806  571 DEIDRMILEIQSMQGKLsKEK 591
Cdd:pfam15619 170 EEVKILQEEIERLQQKL-KEK 189
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
473-624 1.55e-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: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  473 QLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL-ICQKKKE--------KELVTTVQSLQQKVERCLEDGIRLPML 543
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALEAELDALQERReALQRLAEyswdeidvASAEREIAELEAELERLDASSDDLAAL 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  544 DA--KQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKL-SKEKLTTQKMMEELEKK------ERNVQRLTKA 614
Cdd:COG4913   691 EEqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeAAEDLARLELRALLEERfaaalgDAVERELREN 770

                         170
                  ....*....|
gi 767942806  615 LLENQRQTDE 624
Cdd:COG4913   771 LEERIDALRA 780
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 327-626 1.84e-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: 41.63  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  327 QQQQIEDfrqgSETPMQVLTgSSRQSYSPGYQDFSKW----ESMLKIKEGLLRQKEIVIDrQKQQITHLHERIRDNELRA 402
Cdd:pfam05483 368 EQQRLEK----NEDQLKIIT-MELQKKSSELEEMTKFknnkEVELEELKKILAEDEKLLD-EKKQFEKIAEELKGKEQEL 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  403 QHAMLGHYVNCEDSYVASLQLKTRDRYISSLKKKCQKESEqnKEKQRRIETLEKylADLPTLDDVQ-SQSLQLQILEEKN 481
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE--KEKLKNIELTAH--CDKLLLENKElTQEASDMTLELKK 517

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  482 KnlQEALIDTEKKLEEIKKQC---QDKETQLICQ-KKKEKELVTTVQSLQQKVE------RCLEDGIRLPMLDAKQLQNE 551
Cdd:pfam05483 518 H--QEDIINCKKQEERMLKQIenlEEKEMNLRDElESVREEFIQKGDEVKCKLDkseenaRSIEYEVLKKEKQMKILENK 595

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  552 NDNLRQQNETASKIIDSQQDE---------------------IDRMILEIQSMQGKLSK-----------EKLTTQKMME 599
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQEnkalkkkgsaenkqlnayeikVNKLELELASAKQKFEEiidnyqkeiedKKISEEKLLE 675

                         330       340
                  ....*....|....*....|....*..
gi 767942806  600 ELEKKERNVQRLTKAllenQRQTDETC 626
Cdd:pfam05483 676 EVEKAKAIADEAVKL----QKEIDKRC 698
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
430-661 1.93e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 430 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNK--NLQEALIDTE--------------- 492
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKkyNLEELEKKAEeyeklkekliklkge 540

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 493 --------KKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIR---------LPMLDAKQ----LQNE 551
Cdd:PRK03918 541 ikslkkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKelepfyneyLELKDAEKelerEEKE 620

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 552 NDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLttQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLD- 630
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEk 698

                        250       260       270
                 ....*....|....*....|....*....|....
gi 767942806 631 ---QGQEPDQSRQQTVLSKRPLFDLTVIDQLFKE 661
Cdd:PRK03918 699 lkeELEEREKAKKELEKLEKALERVEELREKVKK 732
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
429-661 2.07e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 429 YISSLKKKCQKESEQNKEKQRRIETLEKYLADlpTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQ 508
Cdd:COG4372   25 LIAALSEQLRKALFELDKLQEELEQLREELEQ--AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 509 LICQKKKEKELVTTVQSLQQKVercledgirlpmldaKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLS 588
Cdd:COG4372  103 LESLQEEAEELQEELEELQKER---------------QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942806 589 KEKLTTQKMmeeleKKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPLFDLTVIDQLFKE 661
Cdd:COG4372  168 ALEQELQAL-----SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 439-624 2.12e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   439 KESEQNKEKQRRIETLEKYLADLptLDDVQSQslqlqilEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKE 518
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSL--QSELRRI-------ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   519 LVTTVQSLQQK---VERCLEDGI-RLPMLDAK--QLQNENDNL-----RQQNETASKIIDSQQDEIDRMILEIQSMQGKL 587
Cdd:TIGR02169  742 LEEDLSSLEQEienVKSELKELEaRIEELEEDlhKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 767942806   588 SKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 624
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
381-536 2.22e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 381 IDRQKQQITHLHERIRDNELRAQHAMLGHYVNCEDsyvaslqlktRDRYISSLKKKcqkesEQNKEKQRRIETLEKYLAD 460
Cdd:COG4717  349 LQELLREAEELEEELQLEELEQEIAALLAEAGVED----------EEELRAALEQA-----EEYQELKEELEELEEQLEE 413

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767942806 461 LPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqkkKEKELVTTVQSLQQKVERCLED 536
Cdd:COG4717  414 LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-----EQLEEDGELAELLQELEELKAE 484
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 439-678 2.42e-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: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   439 KESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEeknknlqealiDTEKKLEEIKKQCQDKETQLICQKKKEKE 518
Cdd:TIGR00618  186 FAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLE-----------KELKHLREALQQTQQSHAYLTQKREAQEE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   519 LVTTVQSLQQKVERCLEDGIRLPMLdakQLQNENDNLRQQNE---TASKIIDSQQDEIDRMILEIQSMQGKLSKE---KL 592
Cdd:TIGR00618  255 QLKKQQLLKQLRARIEELRAQEAVL---EETQERINRARKAAplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlmkRA 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   593 TTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLdqgqepDQSRQQTVLSKRplfdltvIDQLFKEMSCCLFDLKAL 672
Cdd:TIGR00618  332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR------EISCQQHTLTQH-------IHTLQQQKTTLTQKLQSL 398


                   ....*.
gi 767942806   673 CSILNQ 678
Cdd:TIGR00618  399 CKELDI 404
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 472-624 2.48e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 472 LQLQILEEKNKNLQEaliDTEKkLEEIKKQCQDKETQlicQKKKEKELvttvQSLQQKVERCLEDGIRLpmldAKQLQNE 551
Cdd:PRK00409 499 LPENIIEEAKKLIGE---DKEK-LNELIASLEELERE---LEQKAEEA----EALLKEAEKLKEELEEK----KEKLQEE 563

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767942806 552 NDNLRQ-QNETASKIIDSQQDEIDRMILEIQSMQgKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 624
Cdd:PRK00409 564 EDKLLEeAEKEAQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 544-631 2.90e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806   544 DAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTT-----QKMMEELEKKERNVQRLTKALLE- 617
Cdd:smart00935   5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLseaarEKKEKELQKKVQEFQRKQQKLQQd 84

                           90
                   ....*....|....*
gi 767942806   618 -NQRQTDETCSLLDQ 631
Cdd:smart00935  85 lQKRQQEELQKILDK 99
PRK11281 PRK11281
mechanosensitive channel MscK;
459-647 3.00e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.05  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  459 ADLPTLDDVQSQSLQLQ---ILEEKNKNLQEALIDT----------EKKLEEIKKQCQDKETQLicqKKKEKELVTTVQS 525
Cdd:PRK11281   33 GDLPTEADVQAQLDALNkqkLLEAEDKLVQQDLEQTlalldkidrqKEETEQLKQQLAQAPAKL---RQAQAELEALKDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  526 LQQKVERCLEDgIRLPMLDAK------QLQNENDNLrqqNETASKIIDSQ------QDEIDRMILEIQSMQ-----GKLS 588
Cdd:PRK11281  110 NDEETRETLST-LSLRQLESRlaqtldQLQNAQNDL---AEYNSQLVSLQtqperaQAALYANSQRLQQIRnllkgGKVG 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767942806  589 KEKLT-TQKMMEELEKKERNVQ-RLTKALLEN--------QRQTDETCSLLDQGQEPDQSRQQTVLSKR 647
Cdd:PRK11281  186 GKALRpSQRVLLQAEQALLNAQnDLQRKSLEGntqlqdllQKQRDYLTARIQRLEHQLQLLQEAINSKR 254
PRK12705 PRK12705
hypothetical protein; Provisional
 475-629 3.85e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.46  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 475 QILEEKNKNLQEALIDTEKKLEEIkkQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEdgiRLPMLDAKQlqNENDN 554
Cdd:PRK12705  30 RLAKEAERILQEAQKEAEEKLEAA--LLEAKELLLRERNQQRQEARREREELQREEERLVQ---KEEQLDARA--EKLDN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 555 LRQQNETASKIIDSQQDEID------RMILE--------------IQSMQGKLSKEKLTTQKMMEE---LEKKERNVQRL 611
Cdd:PRK12705 103 LENQLEEREKALSARELELEelekqlDNELYrvagltpeqarkllLKLLDAELEEEKAQRVKKIEEeadLEAERKAQNIL 182

                        170
                 ....*....|....*...
gi 767942806 612 TKALlenQRQTDETCSLL 629
Cdd:PRK12705 183 AQAM---QRIASETASDL 197
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 564-631 4.88e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 38.66  E-value: 4.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767942806 564 KIIDSQQDEIDRMILEIQSMQGKLSKEKLTT-----QKMMEELEKKERNVQRLTKALLE--NQRQTDETCSLLDQ 631
Cdd:COG2825   50 KEFKKRQAELQKLEKELQALQEKLQKEAATLseeerQKKERELQKKQQELQRKQQEAQQdlQKRQQELLQPILEK 124
PRK12704 PRK12704
phosphodiesterase; Provisional
 432-605 5.84e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 432 SLKKKcqKESEQNKEKQRRIETLEKyladlptldDVQSQSLQLQILEEKNKNLQEALidtEKKLEEIKKqcqdKETQLic 511
Cdd:PRK12704  53 AIKKE--ALLEAKEEIHKLRNEFEK---------ELRERRNELQKLEKRLLQKEENL---DRKLELLEK----REEEL-- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 512 qKKKEKELVTTVQSLQQKVERCledgirlpmldaKQLQNEndnlrqQNETASKIIDSQQDEIDRMILEiqSMQGKLSKEK 591
Cdd:PRK12704 113 -EKKEKELEQKQQELEKKEEEL------------EELIEE------QLQELERISGLTAEEAKEILLE--KVEEEARHEA 171

                        170
                 ....*....|....
gi 767942806 592 LTTQKMMEELEKKE 605
Cdd:PRK12704 172 AVLIKEIEEEAKEE 185
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
422-606 6.36e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 422 QLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLadlptlddvQSQSLQLQ---ILEEKNKNLqEALIDTEKKLEEI 498
Cdd:COG1340   89 ELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ---------QTEVLSPEeekELVEKIKEL-EKELEKAKKALEK 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 499 KKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDgirlpMLDAKQ----LQNENDNLRQQNETASKIIDSQQDEID 574
Cdd:COG1340  159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE-----MIELYKeadeLRKEADELHKEIVEAQEKADELHEEII 233

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767942806 575 RMILEIQSMQGKLS--KEKLTTQKMMEELEKKER 606
Cdd:COG1340  234 ELQKELRELRKELKklRKKQRALKREKEKEELEE 267
Spc42p pfam11544
Spindle pole body component Spc42p; Spc42p is a 42-kD component of the S.cerevisiae spindle ...
 555-614 6.43e-03

Spindle pole body component Spc42p; Spc42p is a 42-kD component of the S.cerevisiae spindle body that localizes to the electron dense central region of the SPB.Spc42p is a phosphoprotein which forms a polymeric layer at the periphery of the SPB central plaque. This functions during SPB duplication and also facilitates the attachment of the SPB to the nuclear membrane.


Pssm-ID: 402925  Cd Length: 72  Bit Score: 35.88  E-value: 6.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  555 LRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKA 614
Cdd:pfam11544   3 LIKQNKELQNKLDEKQEEIDRLNVLVGSLRAKLIKYTELNKKLEDELQQSERSSSSGNSR 62
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 434-634 6.81e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.94  E-value: 6.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 434 KKKCQKESEQNKEKQRRIETLEKYLADLPTlDDVQSQSLQLQILEEKNKNLQEalIDTEKKLEEIKKQCQDKETQLICQK 513
Cdd:COG5185  314 LEEQLAAAEAEQELEESKRETETGIQNLTA-EIEQGQESLTENLEAIKEEIEN--IVGEVELSKSSEELDSFKDTIESTK 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806 514 KKEKELVTTVQSLQQKVERCLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQS-----MQGKLS 588
Cdd:COG5185  391 ESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEesqsrLEEAYD 470

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767942806 589 KEKLTTQKMMEELEKK----ERNVQRLTKALLEN----QRQTDETCSLLDQGQE 634
Cdd:COG5185  471 EINRSVRSKKEDLNEEltqiESRVSTLKATLEKLraklERQLEGVRSKLDQVAE 524
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
 476-603 7.31e-03

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 39.43  E-value: 7.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  476 ILEEKN------KNLQEALIDTEKKLEEIKKqcqDKETqLICQKKKEK--------ELVTTVQSLQQKVERCLEDGIRLP 541
Cdd:pfam15066 382 VILEKNdinktlQNLQEILANTQKHLQESRK---EKET-LQLELKKIKvnyvhlqeRYITEMQQKNKSVSQCLEMDKTLS 457

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767942806  542 MLD--AKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLT-TQKMMEELEK 603
Cdd:pfam15066 458 KKEeeVERLQQLKGELEKATTSALDLLKREKETREQEFLSLQEEFQKHEKENLEeRQKLKSRLEK 522
COG5022 COG5022
Myosin heavy chain [General function prediction only];
361-622 7.88e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 39.68  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  361 SKWESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDnelraqhamlGHYVNCEDSYVASLQLKTrDRYISSLKKKCQK- 439
Cdd:COG5022   850 KFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQE----------LKIDVKSISSLKLVNLEL-ESEIIELKKSLSSd 918

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  440 ESEQNKEKQRRIETLEKYL----ADLPTLDDVQSQSlQLQILEEKNKNLQEA---LIDTEKKLEEIKKQCQDKETQLICQ 512
Cdd:COG5022   919 LIENLEFKTELIARLKKLLnnidLEEGPSIEYVKLP-ELNKLHEVESKLKETseeYEDLLKKSTILVREGNKANSELKNF 997

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942806  513 KKKEKELVTTVQSLQQKVERcledgirlpmldAKQLQNENDNLrqqnETASKIIDSQQDEIDRMiLEIQSMQGKLSKEKL 592
Cdd:COG5022   998 KKELAELSKQYGALQESTKQ------------LKELPVEVAEL----QSASKIISSESTELSIL-KPLQKLKGLLLLENN 1060

                         250       260       270
                  ....*....|....*....|....*....|
gi 767942806  593 TTQKMMEELeKKERNVQRLTKALLENQRQT 622
Cdd:COG5022  1061 QLQARYKAL-KLRRENSLLDDKQLYQLEST 1089
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH