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Conserved domains on  [gi|1370482392|ref|XP_024308026|]
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coiled-coil domain-containing protein 157 isoform X1 [Homo sapiens]

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
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
276-523 2.46e-18

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 356 KMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELDKEKA 435
Cdd:COG1196   317 RLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--------AEEELEELAE 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                  ....*...
gi 1370482392 516 QATTDLRL 523
Cdd:COG1196   467 ELLEEAAL 474
PHA03247 super family cl33720
large tegument protein UL36; Provisional
637-758 3.10e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  637 SSKGTQGATPPVQAKSTSPgPLGRQHLPSSRTGRTLLGQPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPCSQP-SKS 715
Cdd:PHA03247  2863 RRRPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPrPQP 2941
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1370482392  716 LLEGVTHLDTCTQNPIKVLVRLRKRLSPGRGQASSAHQPQERP 758
Cdd:PHA03247  2942 PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
276-523 2.46e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 356 KMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELDKEKA 435
Cdd:COG1196   317 RLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--------AEEELEELAE 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                  ....*...
gi 1370482392 516 QATTDLRL 523
Cdd:COG1196   467 ELLEEAAL 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
277-522 5.43e-14

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: 76.25  E-value: 5.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQagklEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTK 356
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  357 MATLERELKQQRESTQAVEAKAQQLQeegERRAAAERQVQQLEEQVQQLEAQVQLLvgrlegagqqvcwaSTELDKEKAR 436
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELE---AQIEQLKEELKALREALDELRAELTLL--------------NEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  437 VDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQELLQSLQREKQG 513
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRE 905

                   ....*....
gi 1370482392  514 LEQATTDLR 522
Cdd:TIGR02168  906 LESKRSELR 914
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
291-514 4.26e-09

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: 59.52  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 291 EALRAQLEEAegqkdglRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKqqlltetSDLKTKMATLERELKQQRES 370
Cdd:pfam07888  30 ELLQNRLEEC-------LQERAELLQAQEAANRQREKEKERYKRDREQWERQR-------RELESRVAELKEELRQSREK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 371 TQAVEAKAQQLQEEGERRAAAERqvqQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH------- 443
Cdd:pfam07888  96 HEELEEKYKELSASSEELSEEKD---ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeeeae 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 444 QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE-------------QLQSEREQGQCQLRAQQELLQSLQRE 510
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittltqklttahRKEAENEALLEELRSLQERLNASERK 252

                  ....
gi 1370482392 511 KQGL 514
Cdd:pfam07888 253 VEGL 256
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
277-522 4.35e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 277 AEQRKDLTRLskhVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehdkqqlltETSDLKTK 356
Cdd:PRK02224  515 EERREDLEEL---IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE-----------EVAELNSK 580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 357 MATLERE---LKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAgqqvcwASTELDKE 433
Cdd:PRK02224  581 LAELKERiesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA------RIEEARED 654
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 434 KARVDSmvrHQESLQAKqrallkqLDSLDQEREELRGSLDEAEAQRARVEEqLQSEREqgqcQLRAQQELLQSLQREKQG 513
Cdd:PRK02224  655 KERAEE---YLEQVEEK-------LDELREERDDLQAEIGAVENELEELEE-LRERRE----ALENRVEALEALYDEAEE 719

                  ....*....
gi 1370482392 514 LEQATTDLR 522
Cdd:PRK02224  720 LESMYGDLR 728
PHA03247 PHA03247
large tegument protein UL36; Provisional
637-758 3.10e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  637 SSKGTQGATPPVQAKSTSPgPLGRQHLPSSRTGRTLLGQPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPCSQP-SKS 715
Cdd:PHA03247  2863 RRRPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPrPQP 2941
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1370482392  716 LLEGVTHLDTCTQNPIKVLVRLRKRLSPGRGQASSAHQPQERP 758
Cdd:PHA03247  2942 PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
675-709 3.84e-03

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 38.50  E-value: 3.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1370482392 675 QPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPC 709
Cdd:pfam02389   7 QPCQPPPQEPCVPTTKEPCHSKVPEPCNPKVPEPC 41
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
278-367 5.12e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 38.17  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:smart01071  53 YELIMNDHLNKRIDKLLKGLREEELSPETPTYNE-MLAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKL 131
                           90
                   ....*....|
gi 1370482392  358 ATLERELKQQ 367
Cdd:smart01071 132 DELEKEEKKK 141
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
276-523 2.46e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 356 KMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELDKEKA 435
Cdd:COG1196   317 RLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--------AEEELEELAE 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                  ....*...
gi 1370482392 516 QATTDLRL 523
Cdd:COG1196   467 ELLEEAAL 474
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
274-517 4.56e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.14  E-value: 4.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDL 353
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 354 KTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwASTELDKE 433
Cdd:COG1196   340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERL 416
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 434 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQG 513
Cdd:COG1196   417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496

                  ....
gi 1370482392 514 LEQA 517
Cdd:COG1196   497 LEAE 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
276-522 4.12e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.60  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKT 355
Cdd:COG1196   220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----LEELELELEEAQAEEYELLA 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 356 KMATLERELKQQRESTQAVEAKAQQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 435
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

                  ....*..
gi 1370482392 516 QATTDLR 522
Cdd:COG1196   453 ELEEEEE 459
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
277-522 5.43e-14

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: 76.25  E-value: 5.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQagklEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTK 356
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  357 MATLERELKQQRESTQAVEAKAQQLQeegERRAAAERQVQQLEEQVQQLEAQVQLLvgrlegagqqvcwaSTELDKEKAR 436
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELE---AQIEQLKEELKALREALDELRAELTLL--------------NEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  437 VDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQELLQSLQREKQG 513
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRE 905

                   ....*....
gi 1370482392  514 LEQATTDLR 522
Cdd:TIGR02168  906 LESKRSELR 914
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
276-532 8.61e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.36  E-value: 8.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 276 AAEQRkdLTRlskhVEALRAQLEeaeGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqCLSEWEH---DKQQLLTETSD 352
Cdd:COG1196   183 ATEEN--LER----LEDILGELE---RQLEPLERQAEKAERYRELKEELKELEAEL---LLLKLREleaELEELEAELEE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 353 LKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwASTELDK 432
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELAE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 433 EKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQEL--------- 503
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqleelee 407
                         250       260       270
                  ....*....|....*....|....*....|
gi 1370482392 504 -LQSLQREKQGLEQATTDLRLTILELEREL 532
Cdd:COG1196   408 aEEALLERLERLEEELEELEEALAELEEEE 437
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
277-517 3.87e-13

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: 73.17  E-value: 3.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQ-------QLLTE 349
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE----ISRLEQQKQilrerlaNLERQ 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  350 TSDLKTKMATLERELKQQRESTQAVEAKAQQLQE--EGERRAAAERQVQQLEEQVQQLEAQVQL--LVGRLEGAGQQVCW 425
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEELEEQLetLRSKVAQLELQIAS 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  426 ASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER-----EELRGSLDEAEAQRARVEEQLQSEREQ-------- 492
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREEleeaeqal 477
                          250       260       270
                   ....*....|....*....|....*....|
gi 1370482392  493 -----GQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:TIGR02168  478 daaerELAQLQARLDSLERLQENLEGFSEG 507
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
278-533 1.18e-12

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: 71.63  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQeqgaRRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  358 ATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:TIGR02168  750 AQLSKELT---ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  438 DSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQELLQSLQREKQGL 514
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELREL 906
                          250
                   ....*....|....*....
gi 1370482392  515 EQATTDLRLTILELERELE 533
Cdd:TIGR02168  907 ESKRSELRRELEELREKLA 925
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
276-523 3.95e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 3.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKT 355
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAA----ERQVqqleeqvqqleaqvqllvgrlegagqqvcwasTELD 431
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALlerlERLE--------------------------------EELE 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 432 KEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLRAQQELLQSLQREK 511
Cdd:COG1196   425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA-EAAARLLLLLEAEADY 503
                         250
                  ....*....|..
gi 1370482392 512 QGLEQATTDLRL 523
Cdd:COG1196   504 EGFLEGVKAALL 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
276-520 7.48e-12

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: 69.32  E-value: 7.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  276 AAEQRKDLTRLSKHVE------ALRAQLEEAEGQKDGLRKQA--GKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLL 347
Cdd:TIGR02168  195 LNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEElrEELEELQEELKEAEEELEELTAE-LQELEEKLEELR 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  348 TETSDLKTKMATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS 427
Cdd:TIGR02168  274 LEVSELEEEIEELQKELY---ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  428 TELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE---EQLQSEREQGQCQLRAQQELL 504
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKL 430
                          250
                   ....*....|....*.
gi 1370482392  505 QSLQREKQGLEQATTD 520
Cdd:TIGR02168  431 EEAELKELQAELEELE 446
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
292-517 3.36e-11

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: 65.56  E-value: 3.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 292 ALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKTKMATLERELKQQREST 371
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 372 QAVEAKAQQLQEE-GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwastelDKEKARVDSMVRHQESLQAK 450
Cdd:COG4942    93 AELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-------PARREQAEELRADLAELAAL 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 451 QRALLKQLDSLD---QEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:COG4942   166 RAELEAERAELEallAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
280-530 7.47e-11

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: 65.86  E-value: 7.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  280 RKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLE--QALKqeqgARRRQAEEDEQcLSEW---EHDKQQLLTETSDLK 354
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALL----KEKREYEGYEL-LKEKealERQKEAIERQLASLE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  355 TKMATLERELKQQRESTQAVEAKAQQLQEE-----GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTE 429
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  430 LDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDE--AEAQRARVE--------EQLQSEREQGQCQLRA 499
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdKEFAETRDElkdyreklEKLKREINELKRELDR 410
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1370482392  500 QQELLQSLQREKQGLEQATTDLRLTILELER 530
Cdd:TIGR02169  411 LQEELQRLSEELADLNAAIAGIEAKINELEE 441
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
284-525 7.59e-11

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: 65.86  E-value: 7.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  284 TRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWE---HDKQQLLTETSDLKTKMATL 360
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSL 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  361 ERELKQQRESTQAVEAKAQQLQEE-GERRAAAE----RQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 435
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDlHKLEEALNdleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  436 RVDSMVRHqesLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE----------EQLQSEREQGQCQLRAQQELLQ 505
Cdd:TIGR02169  830 YLEKEIQE---LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrdlesrlGDLKKERDELEAQLRELERKIE 906
                          250       260
                   ....*....|....*....|
gi 1370482392  506 SLQREKQGLEQATTDLRLTI 525
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKL 926
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
276-516 1.83e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 64.55  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  276 AAEQRKDLTRLSKHVEALRAQ---LEEAEGQKDGLRKQAGKLEQalkQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSD 352
Cdd:COG4913    230 LVEHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELAR 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  353 LKTKMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwasteldk 432
Cdd:COG4913    307 LEAELERLEARLDALRE--ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL--------- 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  433 ekarvdsmVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSereqgqcqlraqqellqsLQREKQ 512
Cdd:COG4913    376 --------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE------------------LEAEIA 429

                   ....
gi 1370482392  513 GLEQ 516
Cdd:COG4913    430 SLER 433
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
266-522 7.26e-10

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: 61.70  E-value: 7.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 266 PLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgaRRRQAEEDEQclsewehdkQQ 345
Cdd:COG4942    12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA--RRIRALEQEL---------AA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 346 LLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGErraaaerqvqqleeqvqqleaqVQLLVGRlEGAGQqvcw 425
Cdd:COG4942    81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPP----------------------LALLLSP-EDFLD---- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 426 asteldkekarvdsMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE---QLQSEREQGQCQLRAQQE 502
Cdd:COG4942   134 --------------AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAllaELEEERAALEALKAERQK 199
                         250       260
                  ....*....|....*....|
gi 1370482392 503 LLQSLQREKQGLEQATTDLR 522
Cdd:COG4942   200 LLARLEKELAELAAELAELQ 219
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
276-506 8.34e-10

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: 62.39  E-value: 8.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  276 AAEQRKDLT-----RLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC---LSEWEHDKQQLL 347
Cdd:TIGR02169  277 LNKKIKDLGeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLT 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE----GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQV 423
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  424 cwasTELDKEKARVDSMVRHQE-----------SLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEqlqsereq 492
Cdd:TIGR02169  437 ----NELEEEKEDKALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE-------- 504
                          250
                   ....*....|....
gi 1370482392  493 GQCQLRAQQELLQS 506
Cdd:TIGR02169  505 RVRGGRAVEEVLKA 518
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
291-514 4.26e-09

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: 59.52  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 291 EALRAQLEEAegqkdglRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKqqlltetSDLKTKMATLERELKQQRES 370
Cdd:pfam07888  30 ELLQNRLEEC-------LQERAELLQAQEAANRQREKEKERYKRDREQWERQR-------RELESRVAELKEELRQSREK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 371 TQAVEAKAQQLQEEGERRAAAERqvqQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH------- 443
Cdd:pfam07888  96 HEELEEKYKELSASSEELSEEKD---ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeeeae 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 444 QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE-------------QLQSEREQGQCQLRAQQELLQSLQRE 510
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittltqklttahRKEAENEALLEELRSLQERLNASERK 252

                  ....
gi 1370482392 511 KQGL 514
Cdd:pfam07888 253 VEGL 256
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
277-492 1.37e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAlkQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLktk 356
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASSDDL--- 687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  357 mATLERELKQQRESTQAVEAKAQQLQEEgERRAAAERQvqqleeqvqQLEAQVQLLVGRLEGAGQQVC-WASTELDKEKA 435
Cdd:COG4913    688 -AALEEQLEELEAELEELEEELDELKGE-IGRLEKELE---------QAEEELDELQDRLEAAEDLARlELRALLEERFA 756
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482392  436 rvdsmvrhqeslQAKQRALLKQLdsldqeREELRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:COG4913    757 ------------AALGDAVEREL------RENLEERIDALRARLNRAEEELERAMRA 795
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
253-475 1.84e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 1.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  253 QFQQLVQDSMGLRPLpAATVGRWAAEQRKDLtrLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRrqaeed 332
Cdd:COG4913    263 RYAAARERLAELEYL-RAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQIR------ 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  333 eqclsewEHDKQQLltetSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAerqvqqleeqvqqLEAQVQLL 412
Cdd:COG4913    334 -------GNGGDRL----EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE-------------FAALRAEA 389
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370482392  413 VGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEA 475
Cdd:COG4913    390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
291-514 3.26e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 291 EALRAQLEEA-EGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWehdkQQLLTETSDLKTKMATLERELKQQRE 369
Cdd:COG4717    41 AFIRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELRE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 370 STQAVEaKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQllvgRLEGAGQQVCWASTELDKEKARVDSMVRhQESLQA 449
Cdd:COG4717   117 ELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLE-QLSLAT 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482392 450 KQRA--LLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcqlraQQELLQSLQREKQGL 514
Cdd:COG4717   191 EEELqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE-----AAALEERLKEARLLL 252
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
276-510 1.17e-07

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 55.73  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALK-------QEQGARRRQAEEDEQC---------LSEW 339
Cdd:COG3096    363 LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARALCglpdltpenAEDY 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  340 EH---DKQQLLTETS-DLKTKMATLERELKQQRESTQAVEAKAqqlqEEGERRAAAERqvqqlEEQVQQLEAQVQLLVGR 415
Cdd:COG3096    443 LAafrAKEQQATEEVlELEQKLSVADAARRQFEKAYELVCKIA----GEVERSQAWQT-----ARELLRRYRSQQALAQR 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  416 LEGAGQQVcwasTELDKEKARvdsmvrhQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgQC 495
Cdd:COG3096    514 LQQLRAQL----AELEQRLRQ-------QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ-RS 581
                          250
                   ....*....|....*
gi 1370482392  496 QLRAQQELLQSLQRE 510
Cdd:COG3096    582 ELRQQLEQLRARIKE 596
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
275-521 1.39e-07

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: 55.03  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 275 WAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ---EQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 352 DLKTKMATLERELKQQRESTQAVEAKAQQLQEEGErraaaerqvqqleeqvqqleaqvqllvgrlegagqqvcwastELD 431
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE------------------------------------------LLE 425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 432 KEKARVDSMVRHQES----LQAKQRALLKQLDSLDQEREELRGSLDEAEAQRarveEQLQSEREQGQCQLRAQQELLQSL 507
Cdd:TIGR04523 426 KEIERLKETIIKNNSeikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI----NKIKQNLEQKQKELKSKEKELKKL 501
                         250
                  ....*....|....
gi 1370482392 508 QREKQGLEQATTDL 521
Cdd:TIGR04523 502 NEEKKELEEKVKDL 515
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
278-522 1.91e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.39  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC-------LSEWEHDKQQLLTET 350
Cdd:COG4717   122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeelleqlSLATEEELQDLAEEL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 351 SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAER-------------------QVQQLEEQVQQLEAQVQL 411
Cdd:COG4717   202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallgLGGSLLSLILTIAGVLFL 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 412 LVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLD-SLDQEREELR------GSLDEAEAQRARVEE 484
Cdd:COG4717   282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLelldriEELQELLREAEELEE 361
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370482392 485 QLQSEREQGQCQ-------------LRAQQELLQSLQREKQGLEQATTDLR 522
Cdd:COG4717   362 ELQLEELEQEIAallaeagvedeeeLRAALEQAEEYQELKEELEELEEQLE 412
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
342-532 1.97e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 1.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  342 DKQQLLTETSDLKTKMATLER------ELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLeaQVQLLVGR 415
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLERahealeDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAE 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  416 LEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRAL-LKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS------ 488
Cdd:COG4913    297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAAlglplp 376
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1370482392  489 -EREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLTILELEREL 532
Cdd:COG4913    377 aSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
355-523 2.48e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 355 TKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQL--LVGRLEGAGQQVCWASTELDK 432
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 433 EKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:COG4717   151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
                         170
                  ....*....|.
gi 1370482392 513 GLEQATTDLRL 523
Cdd:COG4717   231 QLENELEAAAL 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
339-525 3.80e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 3.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  339 WEHDKQQLLTET----SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEG----ERRAAAERQVQQLEEQVQQLEAQVQ 410
Cdd:COG4913    590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELdalqERREALQRLAEYSWDEIDVASAERE 669
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  411 LL-----VGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAE-----AQRA 480
Cdd:COG4913    670 IAeleaeLERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlarlELRA 749
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1370482392  481 RVEEQLQSEREQGQcQLRAQQELLQSLQREKQGLEQATTDLRLTI 525
Cdd:COG4913    750 LLEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAM 793
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
277-522 4.35e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 277 AEQRKDLTRLskhVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehdkqqlltETSDLKTK 356
Cdd:PRK02224  515 EERREDLEEL---IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE-----------EVAELNSK 580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 357 MATLERE---LKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAgqqvcwASTELDKE 433
Cdd:PRK02224  581 LAELKERiesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA------RIEEARED 654
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 434 KARVDSmvrHQESLQAKqrallkqLDSLDQEREELRGSLDEAEAQRARVEEqLQSEREqgqcQLRAQQELLQSLQREKQG 513
Cdd:PRK02224  655 KERAEE---YLEQVEEK-------LDELREERDDLQAEIGAVENELEELEE-LRERRE----ALENRVEALEALYDEAEE 719

                  ....*....
gi 1370482392 514 LEQATTDLR 522
Cdd:PRK02224  720 LESMYGDLR 728
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
310-519 2.24e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 310 QAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE-GERR 388
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 389 AAAERQVQQLEEQVQQLEAQ-VQLLVGRLEGAgqqvcwaSTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREE 467
Cdd:COG3883    93 RALYRSGGSVSYLDVLLGSEsFSDFLDRLSAL-------SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370482392 468 LRGSLDEAEAQRARVEEQLQSEREqgqcQLRAQQELLQSLQREKQGLEQATT 519
Cdd:COG3883   166 LEAAKAELEAQQAEQEALLAQLSA----EEAAAEAQLAELEAELAAAEAAAA 213
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
277-523 4.07e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.40  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQclsewehdkQQLLTETSDLKTK 356
Cdd:COG3206   171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQL---------AEARAELAEAEAR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 357 MATLERELKQQRESTQAVEAkAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwasteLDKEKAR 436
Cdd:COG3206   242 LAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQR 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 437 VDSMVRHQ-ESLQAKQRALLKQLDSLDQEREElrgsLDEAEAQRARVEEQLQSEREQgqcqlraQQELLQSLQREKQGLE 515
Cdd:COG3206   314 ILASLEAElEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVAREL-------YESLLQRLEEARLAEA 382

                  ....*...
gi 1370482392 516 QATTDLRL 523
Cdd:COG3206   383 LTVGNVRV 390
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
344-517 4.33e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 4.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 344 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERraaaerqvqqleeqvqqLEAQVQLLVGRLEGAGQQV 423
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-----------------LEEELEELNEQLQAAQAEL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 424 CWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ-GQCQLRAQQE 502
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQELQAL 176
                         170
                  ....*....|....*
gi 1370482392 503 LLQSLQREKQGLEQA 517
Cdd:COG4372   177 SEAEAEQALDELLKE 191
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
278-516 5.28e-06

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: 49.97  E-value: 5.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  278 EQRKDLTRLSKHVEALRAQLEEAEGQkdgLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQlltETSDLKTKM 357
Cdd:TIGR00618  219 ERKQVLEKELKHLREALQQTQQSHAY---LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ---ERINRARKA 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  358 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVG------RLEGAGQQVCWASTELD 431
Cdd:TIGR00618  293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsqeiHIRDAHEVATSIREISC 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  432 KEKARVDSMVRHQESLQA-------------KQRALLKQLDSLDQEREELRGSLDEAEA----QRARVEEQLQSEREQGQ 494
Cdd:TIGR00618  373 QQHTLTQHIHTLQQQKTTltqklqslckeldILQREQATIDTRTSAFRDLQGQLAHAKKqqelQQRYAELCAAAITCTAQ 452
                          250       260
                   ....*....|....*....|....*
gi 1370482392  495 CQL---RAQQELLQSLQREKQGLEQ 516
Cdd:TIGR00618  453 CEKlekIHLQESAQSLKEREQQLQT 477
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
281-474 7.27e-06

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: 48.00  E-value: 7.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEqgarRRQAEEDEQCLSEWEHDK--QQLLTETSDLKTKMA 358
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQLGNVRNNKeyEALQKEIESLKRRIS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 359 TLERELKQQREstqAVEAKAQQLQEEGERRAAAErqvqqleeqvqqleaqvqllvgrlegagqqvcwasTELDKEKARVD 438
Cdd:COG1579   107 DLEDEILELME---RIEELEEELAELEAELAELE-----------------------------------AELEEKKAELD 148
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370482392 439 smvrhqeslqAKQRALLKQLDSLDQEREELRGSLDE 474
Cdd:COG1579   149 ----------EELAELEAELEELEAEREELAAKIPP 174
COG5281 COG5281
Phage-related minor tail protein [Mobilome: prophages, transposons];
269-524 8.31e-06

Phage-related minor tail protein [Mobilome: prophages, transposons];


Pssm-ID: 444092 [Multi-domain]  Cd Length: 603  Bit Score: 49.22  E-value: 8.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehDKQQLLT 348
Cdd:COG5281   173 AAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAAS----AAAQALA 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 349 ETSDLKTKMATLERELKQQRESTQAVEAKAQQL--QEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwA 426
Cdd:COG5281   249 ALAAAAAAAALALAAAAELALTAQAEAAAAAAAaaAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALR--A 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 427 STELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQS 506
Cdd:COG5281   327 AAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQA 406
                         250
                  ....*....|....*...
gi 1370482392 507 LQREKQGLEQATTDLRLT 524
Cdd:COG5281   407 ATSAFSGLTDALAGAVTT 424
PTZ00121 PTZ00121
MAEBL; Provisional
277-520 9.85e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 9.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  277 AEQRKDLTRLSKHVEALRA-QLEEAEGQK--DGLRK--------QAGKLEQALKQEQ--GARRRQAEEDEQCLSEWEHDK 343
Cdd:PTZ00121  1518 AEEAKKADEAKKAEEAKKAdEAKKAEEKKkaDELKKaeelkkaeEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEV 1597
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  344 QQLLTETSDLKTKmatlerELKQQREStqavEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEaQVQllvgrlegAGQQV 423
Cdd:PTZ00121  1598 MKLYEEEKKMKAE------EAKKAEEA----KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-ELK--------KAEEE 1658
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  424 CWASTELDKEKARVDSmvRHQESLQAKQRALLKQLDSLDQEREELRGS--LDEAEAQRARVEEQLQSEREQGQCQLraqQ 501
Cdd:PTZ00121  1659 NKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELKKAEEENKIKA---E 1733
                          250
                   ....*....|....*....
gi 1370482392  502 ELLQSLQREKQGLEQATTD 520
Cdd:PTZ00121  1734 EAKKEAEEDKKKAEEAKKD 1752
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
276-490 1.02e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqeqgARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG4717    83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERL----EELEE 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeqvqqleaqvqllvgrlegagqqvcwasteldkekA 435
Cdd:COG4717   154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATE-----------------------------------------E 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482392 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLD--EAEAQRARVEEQLQSER 490
Cdd:COG4717   193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEAR 249
PTZ00121 PTZ00121
MAEBL; Provisional
269-505 1.24e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  269 AATVGRWAAEQRKD-LTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLL 347
Cdd:PTZ00121  1344 AAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwaS 427
Cdd:PTZ00121  1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK----A 1499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  428 TELDK---EKARVDSMVRHQESLQAKQRALLKQLDSLDQER--------EELRGSLDEAEAQRARVEEQLQSEREQGQCQ 496
Cdd:PTZ00121  1500 DEAKKaaeAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579

                   ....*....
gi 1370482392  497 LRAQQELLQ 505
Cdd:PTZ00121  1580 LRKAEEAKK 1588
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
252-517 1.25e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.80  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  252 GQFQQLVQ------DSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAegqkDGLRKQAGKLEQALKQEQGAR 325
Cdd:COG3096    413 IQYQQAVQalekarALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVA----DAARRQFEKAYELVCKIAGEV 488
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  326 RRQA--EEDEQCLSEWEhDKQQLLTETSDLKTKMATLERELKQQREstqaveakAQQLQEEGERRAAAERqvqqleeqvq 403
Cdd:COG3096    489 ERSQawQTARELLRRYR-SQQALAQRLQQLRAQLAELEQRLRQQQN--------AERLLEEFCQRIGQQL---------- 549
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  404 QLEAQVQLLVGRLEgagQQVCWASTELDKEKARVDSMVRHQESLQAKQRAL-------LKQLDSLDQEREELRGSLDEAE 476
Cdd:COG3096    550 DAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawLAAQDALERLREQSGEALADSQ 626
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1370482392  477 AQRARVEEQLQSERE--QGQCQLRAQQellQSLQREKQGLEQA 517
Cdd:COG3096    627 EVTAAMQQLLEREREatVERDELAARK---QALESQIERLSQP 666
PTZ00121 PTZ00121
MAEBL; Provisional
274-392 1.31e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRK-----QAGKLEQALKQEQGARR----RQAEEDEQCLSEWEHDKQ 344
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenKIKAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEALKKEA 1698
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1370482392  345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQ--EEGERRAAAE 392
Cdd:PTZ00121  1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeAEEDKKKAEE 1748
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
267-516 1.34e-05

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 48.68  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  267 LPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR--RQAEEDeqcLSEWEHDKQ 344
Cdd:pfam12128  587 LKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTalKNARLD---LRRLFDEKQ 663
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  345 QLltetSDLKTKmaTLERELKQQRESTQAVEAKAQQLqeEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVc 424
Cdd:pfam12128  664 SE----KDKKNK--ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL- 734
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  425 waSTELDKEKARVDsmvRHQESLQAKQRALLKQLD-------SLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQL 497
Cdd:pfam12128  735 --KAAIAARRSGAK---AELKALETWYKRDLASLGvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRR 809
                          250
                   ....*....|....*....
gi 1370482392  498 RAQQELLQSLQREKQGLEQ 516
Cdd:pfam12128  810 PRLATQLSNIERAISELQQ 828
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
269-506 1.89e-05

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: 48.20  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEgqkDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 348
Cdd:pfam05557  36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAE---EALREQA-ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 349 ETSDLKTKMATLERELKQQRESTQAVEakaQQLQEEGERRAAAERQVQQLEEQVQQLEA---QVQLLVGRLEgagQQVCW 425
Cdd:pfam05557 112 ELSELRRQIQRAELELQSTNSELEELQ---ERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQ---SQEQD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 426 aSTELDKEKARVDSMVRhQESLQAKQRALLKQLDS-------LDQEREELRGSLDEAEAQRARVEEqLQSEREQGQCQLR 498
Cdd:pfam05557 186 -SEIVKNSKSELARIPE-LEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREEAAT-LELEKEKLEQELQ 262

                  ....*...
gi 1370482392 499 AQQELLQS 506
Cdd:pfam05557 263 SWVKLAQD 270
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
278-486 1.96e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEqALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKm 357
Cdd:PRK03918  197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE- 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 358 atlERELKQQRESTQAVEAKAQQ---LQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS---TELD 431
Cdd:PRK03918  275 ---IEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELE 351
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 432 KEKARVDSMVRHQESLqakqRALLKQLDSLDQER-----EELRGSLDEAEAQRARVEEQL 486
Cdd:PRK03918  352 KRLEELEERHELYEEA----KAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEI 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
277-632 2.06e-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: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  277 AEQRKDLTRlsKHVEALRAQLEEAEGQKDGLRKQAgklEQALKqeqgARRRQAEEDEqclseweHDKQQLLTETSDLKTK 356
Cdd:TIGR02168  177 TERKLERTR--ENLDRLEDILNELERQLKSLERQA---EKAER----YKELKAELRE-------LELALLVLRLEELREE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  357 MATLERELKQQRESTQAVEAKAQQLQEEGE--RRAAAERQvqqleeqvqqleAQVQLLVGRLEGAGQqvcwasteldkEK 434
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEelRLEVSELE------------EEIEELQKELYALAN-----------EI 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  435 ARVDSMVRHQeslQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgqcqLRAQQELLQSLQREKQGL 514
Cdd:TIGR02168  298 SRLEQQKQIL---RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELEAELEEL 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  515 EQATTDLRLTIlelereleelkererllvafpdlhrptETQihgpvplgtggRSSSVEsqitcptdsgnvtdhMERQVQS 594
Cdd:TIGR02168  371 ESRLEELEEQL---------------------------ETL-----------RSKVAQ---------------LELQIAS 397
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1370482392  595 NDIRIRVLQEENGRLQSMLSKIREVAQQGGLKLIPQDR 632
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
247-517 2.49e-05

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: 47.58  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 247 LPSSLGQFQQLVQDSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR 326
Cdd:pfam07888  32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 327 RQAEEDEQCLSEWEHDKQQLLTETSDLKT-KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAaERQVQQLEEQVQQL 405
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTlTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-QAKLQQTEEELRSL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 406 EAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQ---ESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARV 482
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEaenEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370482392 483 EEQL-QSEREQGQCQLRAQQELLQ------SLQREKQGLEQA 517
Cdd:pfam07888 271 QAELhQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
277-522 3.00e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ------EQGARRRQAEEDEQCLSEWEHD-------- 342
Cdd:PRK03918  220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREleerieELKKEIEELEEKVKELKELKEKaeeyikls 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 343 --KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEaQVQLLVGRLEGAG 420
Cdd:PRK03918  300 efYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLK 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 421 QQVcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRAR--VEEQLQSEREQGQCqLR 498
Cdd:PRK03918  379 KRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKEL-LE 455
                         250       260
                  ....*....|....*....|....
gi 1370482392 499 AQQELLQSLQREKQGLEQATTDLR 522
Cdd:PRK03918  456 EYTAELKRIEKELKEIEEKERKLR 479
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
278-515 3.32e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQA--------------EEDEQCLSEWEHDK 343
Cdd:PRK03918  321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelerlkkrltgltpEKLEKELEELEKAK 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 344 QQLLTETSDLKTKMATLERELKQQRESTQAVE-AKA------QQLQEEGERRAAAErqvqqleeqvqqLEAQVQLLVGRL 416
Cdd:PRK03918  401 EEIEEEISKITARIGELKKEIKELKKAIEELKkAKGkcpvcgRELTEEHRKELLEE------------YTAELKRIEKEL 468
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 417 EGAGQQVcwasTELDKEKARVDsMVRHQESLQAKQRALLKQLDSLD---------------QEREELRGSLDEAEAQRAR 481
Cdd:PRK03918  469 KEIEEKE----RKLRKELRELE-KVLKKESELIKLKELAEQLKELEeklkkynleelekkaEEYEKLKEKLIKLKGEIKS 543
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370482392 482 VEEQLQSEREQgQCQLRAQQELLQSLQREKQGLE 515
Cdd:PRK03918  544 LKKELEKLEEL-KKKLAELEKKLDELEEELAELL 576
Filament pfam00038
Intermediate filament protein;
288-504 3.89e-05

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 46.45  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 288 KHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ-----EQGARRRQAEEDEqcLSEWEHDKQQLLTETSDLKTKMATLER 362
Cdd:pfam00038  54 KEIEDLRRQLDTLTVERARLQLELDNLRLAAEDfrqkyEDELNLRTSAEND--LVGLRKDLDEATLARVDLEAKIESLKE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 363 EL---------------KQQRESTQAVEAKAQQLQEEG----ERRAA----AERQVQQLEEQVQQLEAQVQLLVGRlegA 419
Cdd:pfam00038 132 ELaflkknheeevrelqAQVSDTQVNVEMDAARKLDLTsalaEIRAQyeeiAAKNREEAEEWYQSKLEELQQAAAR---N 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 420 GQQVCWASTELdkekarvdSMVRHQ-ESLQAKQRALLKQLDSLDQEREEL--RGSLDEAEAQR--ARVEEQLQSEREQGQ 494
Cdd:pfam00038 209 GDALRSAKEEI--------TELRRTiQSLEIELQSLKKQKASLERQLAETeeRYELQLADYQEliSELEAELQETRQEMA 280
                         250
                  ....*....|
gi 1370482392 495 CQLRAQQELL 504
Cdd:pfam00038 281 RQLREYQELL 290
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
432-532 4.21e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  432 KEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE---EQLQSEREQGQCQLRAQQELLQSLQ 508
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100
                   ....*....|....*....|....
gi 1370482392  509 REKQGLEQATTDLRLTILELEREL 532
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDL 774
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
269-524 4.36e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLE---QALKQEQGARRRQAEEDEQCLSEWEHD--- 342
Cdd:PRK02224  365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEdflEELREERDELREREAELEATLRTARERvee 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 343 KQQLLTE------------------TSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeQVQQ 404
Cdd:PRK02224  445 AEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER-------LEER 517
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 405 LEAQVQLLVGRLEGAGQQVCWAStELDKEKARVDSMVRHQESLQAKQR-----------ALLKQLDSLDQEREEL---RG 470
Cdd:PRK02224  518 REDLEELIAERRETIEEKRERAE-ELRERAAELEAEAEEKREAAAEAEeeaeeareevaELNSKLAELKERIESLeriRT 596
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370482392 471 SLDEAEAQRARVEEqLQSEREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLT 524
Cdd:PRK02224  597 LLAAIADAEDEIER-LREKREALAELNDERRERLAEKRERKRELEAEFDEARIE 649
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
326-503 5.16e-05

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


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 45.04  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 326 RRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMAtlERELKQQRESTQAVEAKAQQLQEegERRAAAERqvqqleeqvQQL 405
Cdd:pfam15665  52 KRRIQTLEESLEQHERMKRQALTEFEQYKRRVE--ERELKAEAEHRQRVVELSREVEE--AKRAFEEK---------LES 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 406 EAQVQllvgrlegagqqvcwASTELDKEKARVDSMVRHQ---ESLQAKQRAL--------LKQLDSLDQEREELRGSLDE 474
Cdd:pfam15665 119 FEQLQ---------------AQFEQEKRKALEELRAKHRqeiQELLTTQRAQsasslaeqEKLEELHKAELESLRKEVED 183
                         170       180
                  ....*....|....*....|....*....
gi 1370482392 475 AEAQRARVEEqlQSEREQGQCQLRAQQEL 503
Cdd:pfam15665 184 LRKEKKKLAE--EYEQKLSKAQAFYEREL 210
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
274-517 5.51e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.71  E-value: 5.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqeqgarrrqaeedeqclseweHDKQQLLTETSDL 353
Cdd:pfam01576  426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL----------------------QDTQELLQEETRQ 483
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  354 KTKMATLERELKQQRESTQaveakaQQLQEEGERRAAAERqvqqleeqvqqleaqvqllvgrlegagqQVCWASTELDKE 433
Cdd:pfam01576  484 KLNLSTRLRQLEDERNSLQ------EQLEEEEEAKRNVER----------------------------QLSTLQAQLSDM 529
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  434 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARveeqLQSEREQGQCQLRAQQELLQSLQREKQG 513
Cdd:pfam01576  530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR----LQQELDDLLVDLDHQRQLVSNLEKKQKK 605

                   ....
gi 1370482392  514 LEQA 517
Cdd:pfam01576  606 FDQM 609
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
277-522 5.73e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 5.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 277 AEQRKDLTRLSKHVEALRAQ--------------LEEAEGQKDGLRKQAGKLEQALKQEQGARRR--------------- 327
Cdd:PRK02224  380 EDRREEIEELEEEIEELRERfgdapvdlgnaedfLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgq 459
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 328 ---------QAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLE---------RELKQQRE-STQAVEAKAQQLQEEGERR 388
Cdd:PRK02224  460 pvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaedriERLEERREdLEELIAERRETIEEKRERA 539
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 389 AAAERQVQQLEEQVQQLEAQVQllvgRLEGAGQQVCWASTELDKEKARVDSMVrhqESLqAKQRALLKQLDSLDQEREEL 468
Cdd:PRK02224  540 EELRERAAELEAEAEEKREAAA----EAEEEAEEAREEVAELNSKLAELKERI---ESL-ERIRTLLAAIADAEDEIERL 611
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370482392 469 ---RGSLDEAEAQRarvEEQLQSEREQGQcQLRAQ------QELLQSLQREKQGLEQATTDLR 522
Cdd:PRK02224  612 rekREALAELNDER---RERLAEKRERKR-ELEAEfdeariEEAREDKERAEEYLEQVEEKLD 670
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-510 5.84e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 5.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 348
Cdd:COG4717   286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 349 EtsDLKTKMATLERELKQqrESTQAVEAKAQQLQeegERRAAAERqvqqleeqvqqleaqVQLLVGRLEGAGQQVCWAST 428
Cdd:COG4717   366 E--ELEQEIAALLAEAGV--EDEEELRAALEQAE---EYQELKEE---------------LEELEEQLEELLGELEELLE 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 429 ELDKE--KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELR--GSLDEAEAQRARVEEQLQSEREQGQcQLRAQQELL 504
Cdd:COG4717   424 ALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWA-ALKLALELL 502

                  ....*.
gi 1370482392 505 QSLQRE 510
Cdd:COG4717   503 EEAREE 508
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
276-516 7.17e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.32  E-value: 7.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRK-------QAGKLEQALKQEQGARRRqAEEDEQCLSEwehDKQQLLT 348
Cdd:pfam01576  231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKkireleaQISELQEDLESERAARNK-AEKQRRDLGE---ELEALKT 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  349 ETSDLKTKMATlERELKQQRES---------------------------TQAVEAKAQQLQEEGERRAAAERQVQQLEEQ 401
Cdd:pfam01576  307 ELEDTLDTTAA-QQELRSKREQevtelkkaleeetrsheaqlqemrqkhTQALEELTEQLEQAKRNKANLEKAKQALESE 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  402 VQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRAR 481
Cdd:pfam01576  386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1370482392  482 VEEQLQSEREQGQCQLRAQQEL---LQSLQREKQGLEQ 516
Cdd:pfam01576  466 LESQLQDTQELLQEETRQKLNLstrLRQLEDERNSLQE 503
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
343-521 8.21e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 343 KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleEQVQQLEAQVQLLVGRLEGAGQQ 422
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK---------------NGLVDLSEEAKLLLQQLSELESQ 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 423 VCWASTELDKEKARVDSMVRHQESLQAKQ---------RALLKQLDSLDQEREELRGSLDE-------AEAQRARVEEQL 486
Cdd:COG3206   228 LAEARAELAEAEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQL 307
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370482392 487 QSEREQGQCQLRAQQELLQ----SLQREKQGLEQATTDL 521
Cdd:COG3206   308 QQEAQRILASLEAELEALQareaSLQAQLAQLEARLAEL 346
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
282-387 8.45e-05

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 46.21  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 282 DLTRLSKHVEALRAQLEEAEGQKDGLRKQAgkleQALKQEQGarrrQAEEDEQCLSE----WEHDKQQLLTETSDLKTKM 357
Cdd:pfam05911 703 ELASCTENLESTKSQLQESEQLIAELRSEL----ASLKESNS----LAETQLKCMAEsyedLETRLTELEAELNELRQKF 774
                          90       100       110
                  ....*....|....*....|....*....|
gi 1370482392 358 ATLERELKQQRESTQAVEAKAQQLQEEGER 387
Cdd:pfam05911 775 EALEVELEEEKNCHEELEAKCLELQEQLER 804
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
281-525 8.79e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 8.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRqaeeDEQCLSEWEHDKQ---QLLTETSDLKTKM 357
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK----LELLLSNLKKKIQknkSLESQISELKKQN 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 358 ATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleeqVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQ-----------------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 438 DSMVRHQESL-QAKQRALLK----QLDSLDQEREELRGSLDEAEAQRARVEEQ----------LQSEREQGQCQLRAQQE 502
Cdd:TIGR04523 291 NQLKSEISDLnNQKEQDWNKelksELKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnSESENSEKQRELEEKQN 370
                         250       260       270
                  ....*....|....*....|....*....|
gi 1370482392 503 LLQSLQREKQG-------LEQATTDLRLTI 525
Cdd:TIGR04523 371 EIEKLKKENQSykqeiknLESQINDLESKI 400
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
277-383 1.40e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEqclsewehdkqqlltETSDLKTK 356
Cdd:COG2433   409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR---------------EISRLDRE 473
                          90       100
                  ....*....|....*....|....*..
gi 1370482392 357 MATLERELKQQRESTQAVEAKAQQLQE 383
Cdd:COG2433   474 IERLERELEEERERIEELKRKLERLKE 500
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
278-520 1.54e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgkleQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:COG4372    84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEEL----EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 358 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:COG4372   160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 438 DSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:COG4372   240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319

                  ...
gi 1370482392 518 TTD 520
Cdd:COG4372   320 ALL 322
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
277-484 1.92e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 277 AEQRKDL-TRLSKH-VEALRAQLEEAEGQK---DGLRKQAGKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLLTETS 351
Cdd:PRK03918  502 AEQLKELeEKLKKYnLEELEKKAEEYEKLKeklIKLKGEIKSLKKELEKLEELKKKLAELEKK-LDELEEELAELLKELE 580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 352 DLKTK-MATLERELKQ----QRESTQAVEAKaQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQ----- 421
Cdd:PRK03918  581 ELGFEsVEELEERLKElepfYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysee 659
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370482392 422 ---QVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE 484
Cdd:PRK03918  660 eyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
279-489 1.98e-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: 43.76  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 279 QRKD--LTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT-----ETS 351
Cdd:COG1579    13 QELDseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkEYE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 352 DLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleeqvqqleaqvqllvgrlegagqqvcwasteLD 431
Cdd:COG1579    93 ALQKEIESLKRRISDLEDEILELMERIEELEEE---------------------------------------------LA 127
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370482392 432 KEKARVDSMVRHQESLQAKqrallkqldsLDQEREELRGSLDEAEAQRARVEEQLQSE 489
Cdd:COG1579   128 ELEAELAELEAELEEKKAE----------LDEELAELEAELEELEAEREELAAKIPPE 175
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
270-514 2.08e-04

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: 44.50  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 270 ATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAL----KQEQGARRRQAEEDEQC--LSEWEHDK 343
Cdd:pfam07888 139 KTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVlqLQDTITTL 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 344 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLlvgrlegagqQV 423
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTL----------QL 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 424 CWASTELDKEKARvdsMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQL----RA 499
Cdd:pfam07888 289 ADASLALREGRAR---WAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLsesrRE 365
                         250
                  ....*....|....*...
gi 1370482392 500 QQEL---LQSLQREKQGL 514
Cdd:pfam07888 366 LQELkasLRVAQKEKEQL 383
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
344-515 2.26e-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: 43.37  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 344 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleeqvqqlEAQVQLLVGRLEGAGQQV 423
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE---------------------LEDLEKEIKRLELEIEEV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 424 cwaSTELDKEKAR---------VDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQ 494
Cdd:COG1579    72 ---EARIKKYEEQlgnvrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
                         170       180
                  ....*....|....*....|.
gi 1370482392 495 CQLRAQQELLQSLQREKQGLE 515
Cdd:COG1579   149 EELAELEAELEELEAEREELA 169
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
278-525 2.91e-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: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 278 EQRKDLTRLS-------KHVEaLRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTET 350
Cdd:TIGR04523 195 KLLKLELLLSnlkkkiqKNKS-LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 351 SDL---KTKMATLERELKQqrestqaVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQL-----LVGRLEgagQQ 422
Cdd:TIGR04523 274 KELeqnNKKIKELEKQLNQ-------LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIsqnnkIISQLN---EQ 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 423 VcwasTELDKEKARVDSM-VRHQESLQAKQrallKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLraqQ 501
Cdd:TIGR04523 344 I----SQLKKELTNSESEnSEKQRELEEKQ----NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ-QK---D 411
                         250       260
                  ....*....|....*....|....
gi 1370482392 502 ELLQSLQREKQGLEQATTDLRLTI 525
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETI 435
PHA03247 PHA03247
large tegument protein UL36; Provisional
637-758 3.10e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  637 SSKGTQGATPPVQAKSTSPgPLGRQHLPSSRTGRTLLGQPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPCSQP-SKS 715
Cdd:PHA03247  2863 RRRPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPrPQP 2941
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1370482392  716 LLEGVTHLDTCTQNPIKVLVRLRKRLSPGRGQASSAHQPQERP 758
Cdd:PHA03247  2942 PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
276-519 3.16e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 43.90  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 276 AAEQRKDLTRLSKHVEALRAQLEEA-------EGQKDGLRKQAGKLEQALkQEQGARRRQAEEDEQcLSEWEHDKQQLLT 348
Cdd:pfam19220 106 KEELRIELRDKTAQAEALERQLAAEteqnralEEENKALREEAQAAEKAL-QRAEGELATARERLA-LLEQENRRLQALS 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 349 E-----TSDLKTKMATLERELKQQRESTQAVEAkaqQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQV 423
Cdd:pfam19220 184 EeqaaeLAELTRRLAELETQLDATRARLRALEG---QLAAE---QAERERAEAQLEEAVEAHRAERASLRMKLEALTARA 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 424 cwASTEldkekaRVDSMVRHQ-ESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQsEREQGQCQLRAQQE 502
Cdd:pfam19220 258 --AATE------QLLAEARNQlRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-EMQRARAELEERAE 328
                         250
                  ....*....|....*...
gi 1370482392 503 LL-QSLQREKQGLEQATT 519
Cdd:pfam19220 329 MLtKALAAKDAALERAEE 346
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
267-526 3.19e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 267 LPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEG--QKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQ 344
Cdd:COG1196   540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVC 424
Cdd:COG1196   620 DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 425 WASTELDKE-KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEA-----------EAQRARVEEqLQSEREQ 492
Cdd:COG1196   700 LAEEEEERElAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdlEELERELER-LEREIEA 778
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1370482392 493 -GQCQLRAQQEL------LQSLQREKQGLEQATTDLRLTIL 526
Cdd:COG1196   779 lGPVNLLAIEEYeeleerYDFLSEQREDLEEARETLEEAIE 819
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
299-512 3.29e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 299 EAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEA-- 376
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEIsr 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 377 --KAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTE--------LDKEKARVDSMVRHQES 446
Cdd:pfam17380 377 mrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEarqrevrrLEEERAREMERVRLEEQ 456
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370482392 447 LQAKQRALLKQlDSLDQEREELRGSLDE-----AEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:pfam17380 457 ERQQQVERLRQ-QEEERKRKKLELEKEKrdrkrAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
285-510 3.32e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.40  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  285 RLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAL----------KQEQGARRRQAEEDEQCLSE-------WEHDKQQLL 347
Cdd:pfam01576  549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELddllvdldhqRQLVSNLEKKQKKFDQMLAEekaisarYAEERDRAE 628
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAA-----------ERQVQQLEEQVQQLEAQVQLLVGRL 416
Cdd:pfam01576  629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknvhelERSKRALEQQVEEMKTQLEELEDEL 708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  417 EGAGQQVCWASTELDKEKARVDSMVRHQESL-QAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS------- 488
Cdd:pfam01576  709 QATEDAKLRLEVNMQALKAQFERDLQARDEQgEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqida 788
                          250       260
                   ....*....|....*....|....*
gi 1370482392  489 ---EREQGQCQLRAQQELLQSLQRE 510
Cdd:pfam01576  789 ankGREEAVKQLKKLQAQMKDLQRE 813
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
272-373 3.80e-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: 43.60  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 272 VGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:COG4942   144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
                          90       100
                  ....*....|....*....|..
gi 1370482392 352 DLKTKMATLERELKQQRESTQA 373
Cdd:COG4942   224 ELEALIARLEAEAAAAAERTPA 245
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
290-512 4.46e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 290 VEALRAQLEEAEGQKDGLRKQAGKLEQalkqeqgaRRRQAEEDeqcLSEWEHDKQQLLTETSDLKTKMATLE-------- 361
Cdd:COG1340     3 TDELSSSLEELEEKIEELREEIEELKE--------KRDELNEE---LKELAEKRDELNAQVKELREEAQELRekrdelne 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 362 --RELKQQRESTQaveAKAQQLQEEgerrAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAgQQVcwASTELDKEKARVDS 439
Cdd:COG1340    72 kvKELKEERDELN---EKLNELREE----LDELRKELAELNKAGGSIDKLRKEIERLEWR-QQT--EVLSPEEEKELVEK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 440 MVRHQESLQAKQRA---------LLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLRAQQELLQSLQRE 510
Cdd:COG1340   142 IKELEKELEKAKKAlekneklkeLRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVE 220

                  ..
gi 1370482392 511 KQ 512
Cdd:COG1340   221 AQ 222
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
277-492 4.63e-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: 43.90  E-value: 4.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  277 AEQRKDLTRLSKHVEALRA-----QLEEAEGQKDGLRKQAGKLE---QALKQEQGAR--RRQAEEDE-----QCLSEWEH 341
Cdd:TIGR02169  768 EELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIEarlREIEQKLNRLtlEKEYLEKEiqelqEQRIDLKE 847
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  342 DKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQ 421
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  422 QVCWASTELDKEKARVDSMVRHQ---ESLQAKQRALLKQLDSLD-------QEREELRGSLDEAEAQRARVEEqlqsERE 491
Cdd:TIGR02169  928 ALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEE----ERK 1003

                   .
gi 1370482392  492 Q 492
Cdd:TIGR02169 1004 A 1004
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
445-524 5.34e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 43.79  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  445 ESLQAKQRALLKQLDSLDQEREELRgSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQS---------LQREKQGLE 515
Cdd:PRK11448   145 HALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEkaaetsqerKQKRKEITD 223

                   ....*....
gi 1370482392  516 QATTDLRLT 524
Cdd:PRK11448   224 QAAKRLELS 232
TelA pfam05816
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ...
426-524 5.83e-04

Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like proteins. TelA and KlA are associated with tellurite resistance and plasmid fertility inhibition.


Pssm-ID: 461748  Cd Length: 330  Bit Score: 42.89  E-value: 5.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 426 ASTELDKEKARVDSMVRH----QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQ-----------RARVEEQLQSER 490
Cdd:pfam05816  79 AGNKIEKYFAKYQTAGAQidkiVVELEKGQDELLKDNAMLDQMYEKNLEYFKELEKYiaagelkleelDAELLPELEAKA 158
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1370482392 491 EQGQCQLRAQ--QELLQSLQRekqgLEQATTDLRLT 524
Cdd:pfam05816 159 AASGDPEDAQalRDLRQALFR----LEQRIHDLELQ 190
mukB PRK04863
chromosome partition protein MukB;
286-522 6.19e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 6.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  286 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQaLKQEQGARRrqaeEDEQCLSEWEHDKQQLLTETSDLKTKMATLErELK 365
Cdd:PRK04863   892 LADRVEEIREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQ----SDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVV 965
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  366 QQR-----ESTQAVEAKAQQLQEegerraaaerqvqqleeqvqqleaqvqLLVGRLEGAGQQVCWASTELDKEKARVDSM 440
Cdd:PRK04863   966 QRRahfsyEDAAEMLAKNSDLNE---------------------------KLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  441 VRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARV-EEQL-------QSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:PRK04863  1019 NQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARArRDELharlsanRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
                          250
                   ....*....|
gi 1370482392  513 GLEQATTDLR 522
Cdd:PRK04863  1099 KLERDYHEMR 1108
PTZ00121 PTZ00121
MAEBL; Provisional
274-517 6.60e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  274 RWAAEQRKDLTRlSKHVEALR-----AQLEEAEGQKDGLRKQAGKLEQALKQEQgarRRQAEE----DEQCLSEwEHDKQ 344
Cdd:PTZ00121  1230 KKAEEAKKDAEE-AKKAEEERnneeiRKFEEARMAHFARRQAAIKAEEARKADE---LKKAEEkkkaDEAKKAE-EKKKA 1304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQleeqvqqleaqvqllvgRLEGAGQQVC 424
Cdd:PTZ00121  1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-----------------EAEAAEEKAE 1367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  425 WASTELDKEKARVDSM------VRHQESLQAKQRALLKQLDSLDQEREELRgsldEAEAQRARVEEQLQSEREQGQCQLR 498
Cdd:PTZ00121  1368 AAEKKKEEAKKKADAAkkkaeeKKKADEAKKKAEEDKKKADELKKAAAAKK----KADEAKKKAEEKKKADEAKKKAEEA 1443
                          250
                   ....*....|....*....
gi 1370482392  499 AQQELLQSLQREKQGLEQA 517
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEA 1462
mukB PRK04863
chromosome partition protein MukB;
290-517 6.97e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 6.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  290 VEALRAQLEEAEGQKDGLRKQAGKLEQALK-------QEQGARRRQAEEDEQC-LSEWEHDKQQLLTETSDLKTKMATLE 361
Cdd:PRK04863   378 QEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiQYQQAVQALERAKQLCgLPDLTADNAEDWLEEFQAKEQEATEE 457
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  362 -RELKQQRESTQAVE---AKAQQLQeegeRRAAAERQVQQLEEQVQQLEAQV---QLLVGRLEGAGQQVcwasTELDKEk 434
Cdd:PRK04863   458 lLSLEQKLSVAQAAHsqfEQAYQLV----RKIAGEVSRSEAWDVARELLRRLreqRHLAEQLQQLRMRL----SELEQR- 528
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  435 arvdsmVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgQCQLRAQQELLQSLQREKQGL 514
Cdd:PRK04863   529 ------LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER-RMALRQQLEQLQARIQRLAAR 601

                   ...
gi 1370482392  515 EQA 517
Cdd:PRK04863   602 APA 604
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
272-525 7.78e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 7.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 272 VGRWAAEQRKDLTRLSKHVEA-----LRAQLEEAEGQKDGLRKQAGKLEQalKQEQGARRRqaEEDEQCLSEWEHDKQQL 346
Cdd:PRK02224  178 VERVLSDQRGSLDQLKAQIEEkeekdLHERLNGLESELAELDEEIERYEE--QREQARETR--DEADEVLEEHEERREEL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 347 LT---ETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE-GERRAAAERQVQQL---EEQVQQLEAQVQLLVGRLEGA 419
Cdd:PRK02224  254 ETleaEIEDLRETIAETEREREELAEEVRDLRERLEELEEErDDLLAEAGLDDADAeavEARREELEDRDEELRDRLEEC 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 420 GQQVCWASTELDKEKARVDSmvRHQESLQAKQRAllkqlDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ---GQCQ 496
Cdd:PRK02224  334 RVAAQAHNEEAESLREDADD--LEERAEELREEA-----AELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVD 406
                         250       260
                  ....*....|....*....|....*....
gi 1370482392 497 LRAQQELLQSLQREKQGLEQATTDLRLTI 525
Cdd:PRK02224  407 LGNAEDFLEELREERDELREREAELEATL 435
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
328-517 9.55e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 9.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 328 QAEED-EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLE 406
Cdd:PRK03918  186 KRTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 407 AQVQLLVGRLEGAGQQVCwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEqL 486
Cdd:PRK03918  266 ERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-L 343
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370482392 487 QSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:PRK03918  344 KKKLKELEKRLEELEERHELYEEAKAKKEEL 374
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
343-479 1.00e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 40.71  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 343 KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeqvQQLEAQVQLLVGRLEGAgqq 422
Cdd:PRK07352   52 REAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIR---------AEIEKQAIEDMARLKQT--- 119
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482392 423 vcwASTELDKEKARVDSMVRHQESLQAKQRALlkqldsldqerEELRGSLDEAEAQR 479
Cdd:PRK07352  120 ---AAADLSAEQERVIAQLRREAAELAIAKAE-----------SQLPGRLDEDAQQR 162
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
286-384 1.07e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 286 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgarrRQAEEDEQCLSEWEHDKQQLLTetsdLKTKMATLERELK 365
Cdd:pfam13851  31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQ----EEVEELRKQLENYEKDKQSLKN----LKARLKVLEKELK 102
                          90
                  ....*....|....*....
gi 1370482392 366 QQRESTQAVEAKAQQLQEE 384
Cdd:pfam13851 103 DLKWEHEVLEQRFEKVERE 121
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
281-502 1.08e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQ---GARRRQAEEDEQCLSEWEhdkqQLL--TETSDLKT 355
Cdd:COG3883    44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelGERARALYRSGGSVSYLD----VLLgsESFSDFLD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAErqvqqleeqvQQLEAQVQLLVGRLEgagqqvcwastELDKEKA 435
Cdd:COG3883   120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKL----------AELEALKAELEAAKA-----------ELEAQQA 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482392 436 RVDSMVrhqESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQE 502
Cdd:COG3883   179 EQEALL---AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
274-523 1.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgaRRRQAEEDEQCLSEWE------------- 340
Cdd:COG4717   185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE--NELEAAALEERLKEARlllliaaallall 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 341 --HDKQQLLTET----------------SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQV 402
Cdd:COG4717   263 glGGSLLSLILTiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 403 QQLEAQVQLLVGRLEGAGQQVCWASTELDKE----KARVDS---------MVRHQESLQAKQRALLKQLDSLDQEREEL- 468
Cdd:COG4717   343 LDRIEELQELLREAEELEEELQLEELEQEIAallaEAGVEDeeelraaleQAEEYQELKEELEELEEQLEELLGELEELl 422
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370482392 469 -RGSLDEAEAQRARVEEQLQSEREQgqcqlraQQELLQSLQREKQGLEQATTDLRL 523
Cdd:COG4717   423 eALDEEELEEELEELEEELEELEEE-------LEELREELAELEAELEQLEEDGEL 471
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
276-521 1.48e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  276 AAEQRKDLTRLSKhveALRAQLEEAEGQKDGLRKQAGKLEQ---ALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSD 352
Cdd:pfam01576  648 ALEAKEELERTNK---QLRAEMEDLVSSKDDVGKNVHELERskrALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQA 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  353 LKtkmATLERELKQQREstQAVEAKAQ----------QLQEEGERRAAAerqvqqlEEQVQQLEAQVQLLVGRLEGAGQQ 422
Cdd:pfam01576  725 LK---AQFERDLQARDE--QGEEKRRQlvkqvreleaELEDERKQRAQA-------VAAKKKLELDLKELEAQIDAANKG 792
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  423 VCWASTELDKEKARVDSMVRHQESLQAKQRALL-------KQLDSLdqEREELRGSLDEAEAQRARveEQLQSEREQGQC 495
Cdd:pfam01576  793 REEAVKQLKKLQAQMKDLQRELEEARASRDEILaqskeseKKLKNL--EAELLQLQEDLAASERAR--RQAQQERDELAD 868
                          250       260
                   ....*....|....*....|....*.
gi 1370482392  496 QLRAQQELLQSLQREKQGLEQATTDL 521
Cdd:pfam01576  869 EIASGASGKSALQDEKRRLEARIAQL 894
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
290-524 1.49e-03

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: 42.12  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 290 VEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRE 369
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKE 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 370 STQAVEAKAQQLQE-EGERRAAAE-----RQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH 443
Cdd:pfam10174 532 ECSKLENQLKKAHNaEEAVRTNPEindriRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLR 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 444 QESLQAKQRALLKQLdsldqEREELRGSLDEAEAQRARVEEQLQSEREQgqcQLraqQELLQSLQREKQGLEQatTDLRL 523
Cdd:pfam10174 612 QMKEQNKKVANIKHG-----QQEMKKKGAQLLEEARRREDNLADNSQQL---QL---EELMGALEKTRQELDA--TKARL 678

                  .
gi 1370482392 524 T 524
Cdd:pfam10174 679 S 679
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
294-388 1.55e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 42.25  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  294 RAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEED---EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRES 370
Cdd:PRK11448   141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvalEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220
                           90
                   ....*....|....*...
gi 1370482392  371 TQAVEAKAQQLQEEGERR 388
Cdd:PRK11448   221 ITDQAAKRLELSEEETRI 238
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
281-384 1.72e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 41.12  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKqeqgARRRQAEEDEQCLSEW-EHDKQQLLTETSdlktkmAT 359
Cdd:pfam02841 197 QALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMME----AQERSYQEHVKQLIEKmEAEREQLLAEQE------RM 266
                          90       100
                  ....*....|....*....|....*.
gi 1370482392 360 LERELKQQRE-STQAVEAKAQQLQEE 384
Cdd:pfam02841 267 LEHKLQEQEElLKEGFKTEAESLQKE 292
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
262-468 1.74e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 262 MGLRPLPAATVGRWAAEQRKDLTRLSK---HVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSE 338
Cdd:COG4372    16 FGLRPKTGILIAALSEQLRKALFELDKlqeELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 339 WEHDKQQLLT---ETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGR 415
Cdd:COG4372    96 LAQAQEELESlqeEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE---IAEREEELKELEEQLESLQEELAALEQE 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370482392 416 LEGAGQQVcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREEL 468
Cdd:COG4372   173 LQALSEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
PRK12704 PRK12704
phosphodiesterase; Provisional
294-509 2.00e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 294 RAQLEEAEGQKDGLRKQAGKLEQALKQEQgarRRQAEEdeqclsEWEHDKQQLltetsdlktkmatlERELKQQRESTQA 373
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA---LLEAKE------EIHKLRNEF--------------EKELRERRNELQK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 374 VEAKAQQLQEEGERRAAAerqvqqleeqvqqleaqvqllvgrLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRA 453
Cdd:PRK12704   87 LEKRLLQKEENLDRKLEL------------------------LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370482392 454 LLKQLDSLDQE--REELRGSL-DEAEAQRA----RVEEQLQSEREQgqcqlRAQQELLQSLQR 509
Cdd:PRK12704  143 ELERISGLTAEeaKEILLEKVeEEARHEAAvlikEIEEEAKEEADK-----KAKEILAQAIQR 200
PTZ00121 PTZ00121
MAEBL; Provisional
278-517 2.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  278 EQRKDlTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR----RQAEEDEQC--LSEWEHDKQQLLTETS 351
Cdd:PTZ00121  1082 DAKED-NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeaRKAEDARKAeeARKAEDAKRVEIARKA 1160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  352 D--LKTKMATLERELKQQRESTQAVEA-KAQQLQE-------EGERRAAAERQVQQLEEQVQQLEAQVqllVGRLEGAGQ 421
Cdd:PTZ00121  1161 EdaRKAEEARKAEDAKKAEAARKAEEVrKAEELRKaedarkaEAARKAEEERKAEEARKAEDAKKAEA---VKKAEEAKK 1237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  422 QvcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER--EELRGSLDEAEAQRARVEEQLQ--SEREQGQCQL 497
Cdd:PTZ00121  1238 D---AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKKKADEAKKAEEKKkaDEAKKKAEEA 1314
                          250       260
                   ....*....|....*....|
gi 1370482392  498 RAQQELLQSLQREKQGLEQA 517
Cdd:PTZ00121  1315 KKADEAKKKAEEAKKKADAA 1334
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
241-516 2.61e-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: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  241 LCQSQNLPSSLGQFQQLVQDSMGLRPLPAATVGRWAAEQRKDLTRLSKHvEALRAQLEEAEGQkdglrkqagkleQALKQ 320
Cdd:TIGR00618  371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKKQ------------QELQQ 437
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  321 EQGARRRQAEEDE-QCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE------GERRAAAER 393
Cdd:TIGR00618  438 RYAELCAAAITCTaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgSCIHPNPAR 517
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  394 QVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDS---MVRHQESLQAKQRALLKQ-LDSLDQEREELR 469
Cdd:TIGR00618  518 QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEqmqEIQQSFSILTQCDNRSKEdIPNLQNITVRLQ 597
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370482392  470 GSLD-EAEAQRARVEEQLQSERE-------------QGQCQLRAQQELLqSLQREKQGLEQ 516
Cdd:TIGR00618  598 DLTEkLSEAEDMLACEQHALLRKlqpeqdlqdvrlhLQQCSQELALKLT-ALHALQLTLTQ 657
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
277-532 3.60e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGA------------------------RRRQAEED 332
Cdd:COG1196   480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvligveaayeaaleaalaaalqniVVEDDEVA 559
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 333 EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLL 412
Cdd:COG1196   560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 413 VGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS-ERE 491
Cdd:COG1196   640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEErLEE 719
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1370482392 492 QGQCQLRAQQELLQSLQREKQGLEQATTDLRLTILELEREL 532
Cdd:COG1196   720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
243-521 3.81e-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: 40.86  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 243 QSQNLPSSLGQFQQLVQDSMGLRplpaATVGRWAAEQR---KDLTRLSKHV----EALRAQLEEAEGQKDG-------LR 308
Cdd:pfam05483 280 QDENLKELIEKKDHLTKELEDIK----MSLQRSMSTQKaleEDLQIATKTIcqltEEKEAQMEELNKAKAAhsfvvteFE 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 309 KQAGKLEQALKQEQgaRRRQAEEDEQCLSEWE-HDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGER 387
Cdd:pfam05483 356 ATTCSLEELLRTEQ--QRLEKNEDQLKIITMElQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE 433
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 388 RAAAERQV----QQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKAR-------------------------VD 438
Cdd:pfam05483 434 LKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieltahcdklllenkeltqeasdmTL 513
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 439 SMVRHQESL---QAKQRALLKQLDSLDQEREELRGSLDEaeaqrarVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:pfam05483 514 ELKKHQEDIincKKQEERMLKQIENLEEKEMNLRDELES-------VREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586

                  ....*.
gi 1370482392 516 QATTDL 521
Cdd:pfam05483 587 KQMKIL 592
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
675-709 3.84e-03

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 38.50  E-value: 3.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1370482392 675 QPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPC 709
Cdd:pfam02389   7 QPCQPPPQEPCVPTTKEPCHSKVPEPCNPKVPEPC 41
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
444-516 4.91e-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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.94  E-value: 4.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482392 444 QESLQAKQRALLKQLDSLDQE----REELRGSLDEAEAQRARVEEQLQSEREQGQcqlRAQQELLQSLQREKQGLEQ 516
Cdd:pfam03938  21 QAQLEKKFKKRQAELEAKQKElqklYEELQKDGALLEEEREEKEQELQKKEQELQ---QLQQKAQQELQKKQQELLQ 94
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
347-517 5.02e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.34  E-value: 5.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  347 LTETSDLKTKMATLERELKQQRESTQAVEAKAQ--------------------QLQEEGERRA----------------- 389
Cdd:pfam02463  178 LIEETENLAELIIDLEELKLQELKLKEQAKKALeyyqlkekleleeeyllyldYLKLNEERIDllqellrdeqeeiessk 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  390 ----AAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER 465
Cdd:pfam02463  258 qeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370482392  466 EELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:pfam02463  338 EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
297-516 5.05e-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: 40.33  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 297 LEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMA------TLERELKQQRES 370
Cdd:COG5185   238 FQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAeytksiDIKKATESLEEQ 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 371 TQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEG--AGQQVCWASTELDKEKARVDSMVrhqESLQ 448
Cdd:COG5185   318 LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENivGEVELSKSSEELDSFKDTIESTK---ESLD 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 449 AKQRALLKQLDSL-----------DQEREELRGSLDEAEAQRARVEEQLQ-SEREQGQCQLRAQQELLQSLQREKQGLEQ 516
Cdd:COG5185   395 EIPQNQRGYAQEIlatledtlkaaDRQIEELQRQIEQATSSNEEVSKLLNeLISELNKVMREADEESQSRLEEAYDEINR 474
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
278-367 5.12e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 38.17  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:smart01071  53 YELIMNDHLNKRIDKLLKGLREEELSPETPTYNE-MLAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKL 131
                           90
                   ....*....|
gi 1370482392  358 ATLERELKQQ 367
Cdd:smart01071 132 DELEKEEKKK 141
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
271-514 5.53e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  271 TVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQclsewehdkQQLLTET 350
Cdd:pfam12128  654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQ---------AYWQVVE 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  351 SDLKTKMATLERELKQQREstqAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwastel 430
Cdd:pfam12128  725 GALDAQLALLKAAIAARRS---GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV------- 794
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  431 dkekARVDSMVRHQESLQAKQRALlkQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQRE 510
Cdd:pfam12128  795 ----LRYFDWYQETWLQRRPRLAT--QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCE 868

                   ....
gi 1370482392  511 KQGL 514
Cdd:pfam12128  869 MSKL 872
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
293-517 5.68e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  293 LRAQLEEAE-------GQKDGLRKQAGKLEQALKQEQGARRR-------------QAEED----EQCLSEWEHDKQQLLT 348
Cdd:pfam01576   80 LESRLEEEEersqqlqNEKKKMQQHIQDLEEQLDEEEAARQKlqlekvtteakikKLEEDilllEDQNSKLSKERKLLEE 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  349 ETSDLKTKMATLERELKQQRESTQAVEAKAQQLQE----EGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVC 424
Cdd:pfam01576  160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEErlkkEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  425 WASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQ---SEREQGQCQLRAQQ 501
Cdd:pfam01576  240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEalkTELEDTLDTTAAQQ 319
                          250
                   ....*....|....*.
gi 1370482392  502 ELLQSLQREKQGLEQA 517
Cdd:pfam01576  320 ELRSKREQEVTELKKA 335
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
428-522 7.16e-03

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: 39.23  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  428 TELDKEKARVDSMVrhqESLQAKQRALLKQLDSLDQEREELRgSLDEAEAQRARveEQLQSEREQGQCQLRAQQELlqsl 507
Cdd:smart00787 161 KLLMKELELLNSIK---PKLRDRKDALEEELRQLKQLEDELE-DCDPTELDRAK--EKLKKLLQEIMIKVKKLEEL---- 230
                           90
                   ....*....|....*
gi 1370482392  508 QREKQGLEQATTDLR 522
Cdd:smart00787 231 EEELQELESKIEDLT 245
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
277-507 7.23e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKTK 356
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE----LKELEEQLESLQEELAALEQE 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 357 MATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKAR 436
Cdd:COG4372   173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370482392 437 VDSmvrHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSL 507
Cdd:COG4372   253 EEV---ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
PHA03247 PHA03247
large tegument protein UL36; Provisional
631-758 7.48e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392  631 DRLWSPSSKGTQGATPPVQAKSTSPGPLgrqhlPSSRTGRTLlGQPCTSPPRQPCTSPPrQPCTSPPRQPCTSPSRQPcS 710
Cdd:PHA03247  2565 DRSVPPPRPAPRPSEPAVTSRARRPDAP-----PQSARPRAP-VDDRGDPRGPAPPSPL-PPDTHAPDPPPPSPSPAA-N 2636
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370482392  711 QPSKSLLEGVTHLDTCTQNPIKVLVRLRKRLSpGRGQASSAHQPQERP 758
Cdd:PHA03247  2637 EPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR-RLGRAAQASSPPQRP 2683
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
278-516 8.64e-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: 39.70  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQeqgarrrQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ-------KGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 358 ATLERELKQQREStqaVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAST--------- 428
Cdd:pfam05483 590 KILENKCNNLKKQ---IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDnyqkeiedk 666
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 429 ---------ELDKEKARVDSMVRHQESLQ-------AKQRALLK----QLDSLDQEREELRGSLDEAEAQRARVEEQLQS 488
Cdd:pfam05483 667 kiseeklleEVEKAKAIADEAVKLQKEIDkrcqhkiAEMVALMEkhkhQYDKIIEERDSELGLYKNKEQEQSSAKAALEI 746
                         250       260
                  ....*....|....*....|....*...
gi 1370482392 489 EREQGQCQLRAQQELLQSLQREKQGLEQ 516
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEIEKEEKEKLKM 774
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
278-384 8.68e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKleqaLKQEQGARRRQAEEDEqclsewehDKQQLLTETSDLKTKM 357
Cdd:PRK03918  663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEK----LKEELEEREKAKKELE--------KLEKALERVEELREKV 730
                          90       100
                  ....*....|....*....|....*..
gi 1370482392 358 ATLERELKqqRESTQAVEAKAQQLQEE 384
Cdd:PRK03918  731 KKYKALLK--ERALSKVGEIASEIFEE 755
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
278-511 9.53e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 9.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 278 EQRKDLTRLSKHVE----ALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDL 353
Cdd:COG1340    15 EKIEELREEIEELKekrdELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEK----VKELKEERDELNEKLNEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 354 KTKMATLERELKQQRESTQAVEAKAQQLQE-----------------------EGERRAAAERQVQQLEEQVQQLEAQVQ 410
Cdd:COG1340    91 REELDELRKELAELNKAGGSIDKLRKEIERlewrqqtevlspeeekelvekikELEKELEKAKKALEKNEKLKELRAELK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482392 411 LLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSER 490
Cdd:COG1340   171 ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
                         250       260
                  ....*....|....*....|.
gi 1370482392 491 EQgqcQLRAQQELLQSLQREK 511
Cdd:COG1340   251 KK---QRALKREKEKEELEEK 268
 
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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