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Conserved domains on  [gi|57012336|ref|NP_001008803|]
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keratin, type II cuticular Hb2 [Rattus norvegicus]

Protein Classification

type II keratin( domain architecture ID 12177255)

type II keratin is an intermediate filament-forming protein that provides mechanical support and fulfills a variety of additional functions in epithelial cells

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
95-405 8.12e-130

Intermediate filament protein;


:

Pssm-ID: 425436 [Multi-domain]  Cd Length: 313  Bit Score: 379.26  E-value: 8.12e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    95 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRSCQ-SNMEPLFEGYICALRRQLDCVSGDHGRLEAELCSLQ 173
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEpSRLYSLYEREIRELRRQLDTLTVERARLQLELDNLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   174 EALEGYKKKYEEELSLRPCAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLKALFEEEISLLQSQISETSVIVKMD 253
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRQSAEADIVGLRKDLDEATLARVDLEMKIESLKEELAFLKKNHEEEVRELQSQVSDTQVNVEMD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   254 NSRDLDVDGIVAEIKAQYDDIASRSKAEAEAWYQCRYEELRMTAGNHSDNLRNRKNEILEMNKLIQRLQQDIETVKAQRC 333
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAEKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQKA 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57012336   334 KLEGAIAQAEQQGEAALSDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 405
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
18-91 2.86e-13

Keratin type II head;


:

Pssm-ID: 435217 [Multi-domain]  Cd Length: 159  Bit Score: 67.38  E-value: 2.86e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57012336    18 GVGGGLRALGCLGSrslcnvGFG-RPRVASRCGMPGFGYRAGAacGSPAC----ITPVTINESLLVPLELEIDPTVQSV 91
Cdd:pfam16208  89 GAGGGFGGGGGFGG------GFGgGGGGGGGFGGGGFGGRGGF--GGPPCppggIQEVTVNQSLLQPLNLEIDPEIQRV 159
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
95-405 8.12e-130

Intermediate filament protein;


Pssm-ID: 425436 [Multi-domain]  Cd Length: 313  Bit Score: 379.26  E-value: 8.12e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    95 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRSCQ-SNMEPLFEGYICALRRQLDCVSGDHGRLEAELCSLQ 173
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEpSRLYSLYEREIRELRRQLDTLTVERARLQLELDNLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   174 EALEGYKKKYEEELSLRPCAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLKALFEEEISLLQSQISETSVIVKMD 253
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRQSAEADIVGLRKDLDEATLARVDLEMKIESLKEELAFLKKNHEEEVRELQSQVSDTQVNVEMD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   254 NSRDLDVDGIVAEIKAQYDDIASRSKAEAEAWYQCRYEELRMTAGNHSDNLRNRKNEILEMNKLIQRLQQDIETVKAQRC 333
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAEKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQKA 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57012336   334 KLEGAIAQAEQQGEAALSDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 405
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
18-91 2.86e-13

Keratin type II head;


Pssm-ID: 435217 [Multi-domain]  Cd Length: 159  Bit Score: 67.38  E-value: 2.86e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57012336    18 GVGGGLRALGCLGSrslcnvGFG-RPRVASRCGMPGFGYRAGAacGSPAC----ITPVTINESLLVPLELEIDPTVQSV 91
Cdd:pfam16208  89 GAGGGFGGGGGFGG------GFGgGGGGGGGFGGGGFGGRGGF--GGPPCppggIQEVTVNQSLLQPLNLEIDPEIQRV 159
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
97-417 1.41e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 63.97  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   97 EQIKCLNNRFASFINKVRFLEQKNKLLETKWNfmqqqrscqsnmeplfegyicALRRQLDCVSGDHGRLEAELCSLQEAL 176
Cdd:COG1196  674 EELAELEAQLEKLEEELKSLKNELRSLEDLLE---------------------ELRRQLEELERQLEELKRELAALEEEL 732
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  177 EGYKKKYEEelslrpcAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLKALFEEEISLLQSQISETSVIVKMDNSR 256
Cdd:COG1196  733 EQLQSRLEE-------LEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEA 805
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  257 DLDVDGIVAEIKAQYDDIASRSKAEAEAW-----YQCRYEELRMTAGNHSDNLRNRKNEILEMNKLIQRLQQDIETVKAQ 331
Cdd:COG1196  806 ERRLDALERELESLEQRRERLEQEIEELEeeieeLEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEE 885
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  332 RCKLEGAIAQAEQQgeaaLSDAKCKLAGLEEALQKAKQDMACL---LKEYQEVMNSKLGLDIEIATYRRLLEGEEhrLCE 408
Cdd:COG1196  886 KEELEEELRELESE----LAELKEEIEKLRERLEELEAKLERLeveLPELEEELEEEYEDTLETELEREIERLEE--EIE 959

                 ....*....
gi 57012336  409 GIGPVNISV 417
Cdd:COG1196  960 ALGPVNLRA 968
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
164-406 9.94e-10

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: 61.23  E-value: 9.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    164 RLEAELCSLQEALEGYKKKYEEelslrpcAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLKAL----------FE 233
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskelteLE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    234 EEISLLQSQISETSVIVKMDNSRDLDVDGIVAEIKAQYDDIASRSKAEaeawyQCRYEELRMTAGNHSDNLRNRKNEILE 313
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-----RAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    314 MNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEAALSdakcKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIA 393
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----ELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          250
                   ....*....|...
gi 57012336    394 TYRRLLEGEEHRL 406
Cdd:TIGR02168  912 ELRRELEELREKL 924
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
80-403 8.61e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 8.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   80 LELEIDPTVQSVKRDE--KEQIKCLNNRFASFINKVRFLEQKNKLLETKwnfMQQQRSCQSNMEPLFEgYICALRRQLDC 157
Cdd:PRK03918 174 IKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREE---LEKLEKEVKELEELKE-EIEELEKELES 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  158 VSGDHGRLEAELCSLQEALEGYKKKYEE------EL-SLRPCAEnEFVTLKKdvdtaFLVKadletnLEALEHEIEFLKA 230
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEEleekvkELkELKEKAE-EYIKLSE-----FYEE------YLDELREIEKRLS 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  231 LFEEEISLLQSQISETSvivkMDNSRdldvdgiVAEIKAQYDDIaSRSKAEAEAWYQcRYEELRMTAGNhSDNLRNR--- 307
Cdd:PRK03918 318 RLEEEINGIEERIKELE----EKEER-------LEELKKKLKEL-EKRLEELEERHE-LYEEAKAKKEE-LERLKKRltg 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  308 ------KNEILEMNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEaALSDAK--CKLAGLE-------EALQKAKQDMA 372
Cdd:PRK03918 384 ltpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-ELKKAKgkCPVCGRElteehrkELLEEYTAELK 462
                        330       340       350
                 ....*....|....*....|....*....|.
gi 57012336  373 CLLKEYQEVMNSKLGLDIEIATYRRLLEGEE 403
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKES 493
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
95-405 8.12e-130

Intermediate filament protein;


Pssm-ID: 425436 [Multi-domain]  Cd Length: 313  Bit Score: 379.26  E-value: 8.12e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    95 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRSCQ-SNMEPLFEGYICALRRQLDCVSGDHGRLEAELCSLQ 173
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEpSRLYSLYEREIRELRRQLDTLTVERARLQLELDNLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   174 EALEGYKKKYEEELSLRPCAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLKALFEEEISLLQSQISETSVIVKMD 253
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRQSAEADIVGLRKDLDEATLARVDLEMKIESLKEELAFLKKNHEEEVRELQSQVSDTQVNVEMD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   254 NSRDLDVDGIVAEIKAQYDDIASRSKAEAEAWYQCRYEELRMTAGNHSDNLRNRKNEILEMNKLIQRLQQDIETVKAQRC 333
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAEKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQKA 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57012336   334 KLEGAIAQAEQQGEAALSDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 405
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
18-91 2.86e-13

Keratin type II head;


Pssm-ID: 435217 [Multi-domain]  Cd Length: 159  Bit Score: 67.38  E-value: 2.86e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57012336    18 GVGGGLRALGCLGSrslcnvGFG-RPRVASRCGMPGFGYRAGAacGSPAC----ITPVTINESLLVPLELEIDPTVQSV 91
Cdd:pfam16208  89 GAGGGFGGGGGFGG------GFGgGGGGGGGFGGGGFGGRGGF--GGPPCppggIQEVTVNQSLLQPLNLEIDPEIQRV 159
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
97-417 1.41e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 63.97  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   97 EQIKCLNNRFASFINKVRFLEQKNKLLETKWNfmqqqrscqsnmeplfegyicALRRQLDCVSGDHGRLEAELCSLQEAL 176
Cdd:COG1196  674 EELAELEAQLEKLEEELKSLKNELRSLEDLLE---------------------ELRRQLEELERQLEELKRELAALEEEL 732
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  177 EGYKKKYEEelslrpcAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLKALFEEEISLLQSQISETSVIVKMDNSR 256
Cdd:COG1196  733 EQLQSRLEE-------LEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEA 805
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  257 DLDVDGIVAEIKAQYDDIASRSKAEAEAW-----YQCRYEELRMTAGNHSDNLRNRKNEILEMNKLIQRLQQDIETVKAQ 331
Cdd:COG1196  806 ERRLDALERELESLEQRRERLEQEIEELEeeieeLEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEE 885
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  332 RCKLEGAIAQAEQQgeaaLSDAKCKLAGLEEALQKAKQDMACL---LKEYQEVMNSKLGLDIEIATYRRLLEGEEhrLCE 408
Cdd:COG1196  886 KEELEEELRELESE----LAELKEEIEKLRERLEELEAKLERLeveLPELEEELEEEYEDTLETELEREIERLEE--EIE 959

                 ....*....
gi 57012336  409 GIGPVNISV 417
Cdd:COG1196  960 ALGPVNLRA 968
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
164-406 9.94e-10

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: 61.23  E-value: 9.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    164 RLEAELCSLQEALEGYKKKYEEelslrpcAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLKAL----------FE 233
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskelteLE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    234 EEISLLQSQISETSVIVKMDNSRDLDVDGIVAEIKAQYDDIASRSKAEaeawyQCRYEELRMTAGNHSDNLRNRKNEILE 313
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-----RAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    314 MNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEAALSdakcKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIA 393
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----ELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          250
                   ....*....|...
gi 57012336    394 TYRRLLEGEEHRL 406
Cdd:TIGR02168  912 ELRRELEELREKL 924
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
151-405 1.10e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.80  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  151 LRRQLDCVSGDHGRLEAELCSLQEALEGYKKKYEEELSLRPCAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLK- 229
Cdd:COG1196  237 LRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELEn 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  230 ---------ALFEEEISLLQSQISETSVIVKMDNSRDLDVDGIVAEIKAQYDDIASRSKAEAEAWYQcRYEELRMTAGNH 300
Cdd:COG1196  317 eleeleerlEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALRE-ELAELEAELAEI 395
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  301 SDNLRNRKNEI-------LEMNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQG---EAALSDAKCKLAGLEEALQKAKQD 370
Cdd:COG1196  396 RNELEELKREIesleerlERLSERLEDLKEELKELEAELEELQTELEELNEELeelEEQLEELRDRLKELERELAELQEE 475
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 57012336  371 MACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 405
Cdd:COG1196  476 LQRLEKELSSLEARLDRLEAEQRASQGVRAVLEAL 510
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
150-403 2.29e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 56.65  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  150 ALRRQLDCVSGDHGRLEAELCSLQEALEGYKKKYEEELSLRPCAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLK 229
Cdd:COG1196  671 ELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELE 750
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  230 A---LFEEEISLLQSQISETSVIVKMDNSRDLDVDGIVAEIKAQYDDIasrskAEAEAWYQCRYEELRMTAGNHSDNLRN 306
Cdd:COG1196  751 EeleELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEEL-----EEELEEAERRLDALERELESLEQRRER 825
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  307 RKNEILEMNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEAALSdakcKLAGLEEALQKAKQDMACLLKEYQEVMNSKL 386
Cdd:COG1196  826 LEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEA----EKEELEDELKELEEEKEELEEELRELESELA 901
                        250
                 ....*....|....*..
gi 57012336  387 GLDIEIATYRRLLEGEE 403
Cdd:COG1196  902 ELKEEIEKLRERLEELE 918
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
80-403 8.61e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 8.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   80 LELEIDPTVQSVKRDE--KEQIKCLNNRFASFINKVRFLEQKNKLLETKwnfMQQQRSCQSNMEPLFEgYICALRRQLDC 157
Cdd:PRK03918 174 IKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREE---LEKLEKEVKELEELKE-EIEELEKELES 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  158 VSGDHGRLEAELCSLQEALEGYKKKYEE------EL-SLRPCAEnEFVTLKKdvdtaFLVKadletnLEALEHEIEFLKA 230
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEEleekvkELkELKEKAE-EYIKLSE-----FYEE------YLDELREIEKRLS 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  231 LFEEEISLLQSQISETSvivkMDNSRdldvdgiVAEIKAQYDDIaSRSKAEAEAWYQcRYEELRMTAGNhSDNLRNR--- 307
Cdd:PRK03918 318 RLEEEINGIEERIKELE----EKEER-------LEELKKKLKEL-EKRLEELEERHE-LYEEAKAKKEE-LERLKKRltg 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  308 ------KNEILEMNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEaALSDAK--CKLAGLE-------EALQKAKQDMA 372
Cdd:PRK03918 384 ltpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-ELKKAKgkCPVCGRElteehrkELLEEYTAELK 462
                        330       340       350
                 ....*....|....*....|....*....|.
gi 57012336  373 CLLKEYQEVMNSKLGLDIEIATYRRLLEGEE 403
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKES 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
150-406 1.50e-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: 47.74  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    150 ALRRQLDCVSGDHGRLEAELCSLQEALEGYKKKYEEELSLRPCAENEFVTLKKDVDtaflvkaDLETNLEALEHEIEFLK 229
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY-------ALANEISRLEQQKQILR 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    230 alfeEEISLLQSQISETSVIVKMDNSRDLDVDGIVAEIKAQYDDIASRSKAEAEAwyqcryeelrmtagnhsdnLRNRKN 309
Cdd:TIGR02168  309 ----ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-------------------LEELEA 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    310 EILEMNKLIQRLQQDIETVKAqrcklegAIAQAEQQGEAA---LSDAKCKLAGLEEALQKAKQDMACLLKEYQEvmNSKL 386
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRS-------KVAQLELQIASLnneIERLEARLERLEDRRERLQQEIEELLKKLEE--AELK 436
                          250       260
                   ....*....|....*....|
gi 57012336    387 GLDIEIATYRRLLEGEEHRL 406
Cdd:TIGR02168  437 ELQAELEELEEELEELQEEL 456
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
80-318 1.67e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.40  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   80 LELEIDPTVQSVKRDeKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRSCQSNMEPLFEGYICALRRQLDcvs 159
Cdd:COG1196  763 LEEELESLEEALAKL-KEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIE--- 838
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  160 gdhgRLEAELCSLQEALEGYKKKYEEELSLRPCAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLK---ALFEEEI 236
Cdd:COG1196  839 ----ELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKeeiEKLRERL 914
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  237 SLLQSQISETSVIVKMDNSR--DLDVDGIVAEIKAQYDDIASRSKA------EAEAWY---QCRYEELRMTAGNHSDNLR 305
Cdd:COG1196  915 EELEAKLERLEVELPELEEEleEEYEDTLETELEREIERLEEEIEAlgpvnlRAIEEYeevEERYEELKSQREDLEEAKE 994
                        250
                 ....*....|...
gi 57012336  306 NRKNEILEMNKLI 318
Cdd:COG1196  995 KLLEVIEELDKEK 1007
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
151-406 4.45e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 46.25  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  151 LRRQLDcvsgdhgRLEAELCSLQEALEgyKKKYEEELSLRpCAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEflka 230
Cdd:COG1196  198 LEKQLE-------KLERQAEKAERYQE--LKAELRELELA-LLLAKLKELRKELEELEEELSRLEEELEELQEELE---- 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  231 LFEEEISLLQSQISETSVIVKMDNSRDLDVDGIVAEIKAQYDDIASRSKAEAEawyqcRYEELRMTagnhsdnLRNRKNE 310
Cdd:COG1196  264 EAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELEN-----ELEELEER-------LEELKEK 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  311 ILEMNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEAALSDakcklagLEEALQKAKQDMACLLKEYQEVMNSKLGLDI 390
Cdd:COG1196  332 IEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEE-------LEELFEALREELAELEAELAEIRNELEELKR 404
                        250
                 ....*....|....*.
gi 57012336  391 EIATYRRLLEGEEHRL 406
Cdd:COG1196  405 EIESLEERLERLSERL 420
46 PHA02562
endonuclease subunit; Provisional
72-377 5.60e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.78  E-value: 5.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   72 INE-SLLVPLELEIDPTVQSVKRDEKE---QIKCLNNRF---ASFINKVRFLEQKNKLLETKWN------------FMQ- 131
Cdd:PHA02562  68 INKkDLLVELWFEYGEKEYYIKRGIKPnvfEIYCNGKLLdesASSKDFQKYFEQMLGMNYKSFKqivvlgtagyvpFMQl 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  132 ---QQR---------SCQSNMEPLFEGYICALRRQLDCvsgdhgrLEAELCSLQEALEGYKKkYEEELSLRPCAENEFVT 199
Cdd:PHA02562 148 sapARRklvedlldiSVLSEMDKLNKDKIRELNQQIQT-------LDMKIDHIQQQIKTYNK-NIEEQRKKNGENIARKQ 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  200 LKKD--VDTAFLVKADL-ETNLEALEHEIEF------LKALfEEEISLLQSQISETSVIVKMDNSRDL---------DVD 261
Cdd:PHA02562 220 NKYDelVEEAKTIKAEIeELTDELLNLVMDIedpsaaLNKL-NTAAAKIKSKIEQFQKVIKMYEKGGVcptctqqisEGP 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  262 GIVAEIKAQYDDIasrskaeaeawyQCRYEELRmtagNHSDNLRNRKNEILEMNKLIQRLQQDIETVKAQRCKLEGAIAQ 341
Cdd:PHA02562 299 DRITKIKDKLKEL------------QHSLEKLD----TAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKK 362
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 57012336  342 AE---QQGEAALSDAKCKLAGLEEALQKAKQDMACLLKE 377
Cdd:PHA02562 363 VKaaiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
166-382 1.95e-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: 429718 [Multi-domain]  Cd Length: 488  Bit Score: 43.72  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   166 EAELCSLQEALEGYKKKYEEELSLRPCAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLkALFEEEISLLQSQISE 245
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERL-NASERKVEGLGEELSS 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   246 T-----SVIVKMDNSRdLDVdgivAEIKAQYDDIASRSKAEAEAWYQCRyEELRMTAgnhsdnlRNRKNEILEMNKLIQR 320
Cdd:pfam07888 263 MaaqrdRTQAELHQAR-LQA----AQLTLQLADASLALREGRARWAQER-ETLQQSA-------EADKDRIEKLSAELQR 329
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57012336   321 LQQDIETVKAQRCKLEGAIAQAEQQGEAALSDAKCKLAGLEEALQKAKQDMACLLKEYQEVM 382
Cdd:pfam07888 330 LEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELL 391
PRK01156 PRK01156
chromosome segregation protein; Provisional
168-403 2.11e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.12  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  168 ELCSLQEALEGYK-KKYEEELSLRPCAENEFVTLKKDVDTAflvkADLETNLEALEHE-----IEFLKALFEEEISLLqS 241
Cdd:PRK01156 501 DLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINEL----KDKHDKYEEIKNRykslkLEDLDSKRTSWLNAL-A 575
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  242 QISetsvivkmdnsrDLDVDGIVA---EIKAQYDDIASRSK------AEAEAWYQCRYEELRmtagNHSDNLRNRKNEIL 312
Cdd:PRK01156 576 VIS------------LIDIETNRSrsnEIKKQLNDLESRLQeieigfPDDKSYIDKSIREIE----NEANNLNNKYNEIQ 639
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  313 EMNKLIQRLQQDIETVKAQRCKLEGaIAQAEQQGEAALSDAKCKLAGLEEALQKAKQDMAcLLKEYQEVMNSKLG-LDIE 391
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQIAEIDS-IIPDLKEITSRINDIEDNLKKSRKALDDAKANRA-RLESTIEILRTRINeLSDR 717
                        250
                 ....*....|..
gi 57012336  392 IATYRRLLEGEE 403
Cdd:PRK01156 718 INDINETLESMK 729
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
164-408 2.14e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 43.98  E-value: 2.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 164 RLEAELCSLQEALEGYKKKYEEELSLRpcaENEFVTLKKdvdtafLVKADLETNLEALEHEIEFLKALFEEEISLLQSQI 243
Cdd:COG0419 182 EAKAKIEELEGQLSELLEDIEDLLEAL---EEELKELKK------LEEIQEEQEEEELEQEIEALEERLAELEEEKERLE 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 244 SETSVIVKMDNSRDLDVDGI---VAEIKAQYDDIASRSKA------EAEAWYQcRYEELRMTAGNHS---DNLRNRKNEI 311
Cdd:COG0419 253 ELKARLLEIESLELEALKIReeeLRELERLLEELEEKIERleelerEIEELEE-ELEGLRALLEELEellEKLKSLEERL 331
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 312 LEMNKLIQRLQQDIE-------TVKAQRCKLEGAIAQAEQQGEAALSDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNS 384
Cdd:COG0419 332 EKLEEKLEKLESELEelaeeknELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEE 411
                       250       260
                ....*....|....*....|....
gi 57012336 385 KLGLDIEIATYRRLLEGEEHRLCE 408
Cdd:COG0419 412 LEELEKELEELERELEELEEEIKK 435
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
150-396 2.31e-04

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 43.47  E-value: 2.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 150 ALRRQLDCVSGDHGRLEAELCSLQEALEgyKKKYEEELslrpcAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLK 229
Cdd:COG4372  85 ALRTELGTAQGEKRAAETEREAARSELQ--KARQEREA-----VRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLA 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 230 ALFEEEISLLQSQISETSvivkmdnsrdlDVDGIVAEIKAQYDDIASRSKaeaeawyqcRYEELRMTAGNHSDNLRNRKN 309
Cdd:COG4372 158 EQRRQLEAQAQSLQASQK-----------QLQASATQLKSQVLDLKLRSA---------QIEQEAQNLATRANAAQARTE 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 310 EILEMNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEAALSdakcKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGld 389
Cdd:COG4372 218 ELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERER----QLQRLETAQARLEQEVAQLEAYYQAYVRLRQQ-- 291

                ....*..
gi 57012336 390 iEIATYR 396
Cdd:COG4372 292 -AAATQR 297
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
150-400 3.48e-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: 43.13  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    150 ALRRQLDCVSGDHGRLEAELCSLQEALEGYKKKYEEelslrpcAENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLK 229
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGE-------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    230 AL---FEEEISLLQSQISEtsVIVKMDNSRDLDVDGIVAEIKAQYDDIasrsKAEAEAWyqcryeELRMTAGNHSDNLRN 306
Cdd:TIGR02169  758 SElkeLEARIEELEEDLHK--LEEALNDLEARLSHSRIPEIQAELSKL----EEEVSRI------EARLREIEQKLNRLT 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    307 RKNEILEmnKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGE---AALSDAKCKLAGLEEALQKAKQDMACLLKEYQEVMN 383
Cdd:TIGR02169  826 LEKEYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
                          250
                   ....*....|....*..
gi 57012336    384 SKLGLDIEIATYRRLLE 400
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLS 920
46 PHA02562
endonuclease subunit; Provisional
237-403 3.48e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.08  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  237 SLLQSQISETSvivkmDNSRDLDV--DGIVAEIKAQYDDIASRSKAEAE--AWYQCRYEELRMTAGNHSDNLRNRKNEIL 312
Cdd:PHA02562 170 KLNKDKIRELN-----QQIQTLDMkiDHIQQQIKTYNKNIEEQRKKNGEniARKQNKYDELVEEAKTIKAEIEELTDELL 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  313 E-----------MNKLIQ---RLQQDIETV--------KAQRCKlegAIAQAEQQGEAALSDAKCKLAGLE---EALQKA 367
Cdd:PHA02562 245 NlvmdiedpsaaLNKLNTaaaKIKSKIEQFqkvikmyeKGGVCP---TCTQQISEGPDRITKIKDKLKELQhslEKLDTA 321
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 57012336  368 KQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEE 403
Cdd:PHA02562 322 IDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
80-392 3.89e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    80 LELEIDPTVQSVKRDEKEQIKclnnrfasFINKVRFLEQKNKLLETKWNFMQQQRSCQSNMEPLFEGYICALRRQLDCVS 159
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDK--------FLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   160 GDHGRLEAELCSLQEALEGYKKKYEEELSLrpcaENEFVTLKKDVDTAFLVKADLETNLEALEHEIEFLKALFEEEISLL 239
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISEL----KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   240 QSQISEtsviVKMDNSRDLDVDGIVAEIKAQYDDIasrSKAEAEAWYQCRYEELRmtagNHSDNLRNRKNEILEMNKLIQ 319
Cdd:TIGR04523 270 SEKQKE----LEQNNKKIKELEKQLNQLKSEISDL---NNQKEQDWNKELKSELK----NQEKKLEEIQNQISQNNKIIS 338
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57012336   320 RLQQDIETVKAQRCKLEgaiaqaeqqgeaalSDAKCKLAGLEEALQKAKQdmacLLKEYQEVMNSKLGLDIEI 392
Cdd:TIGR04523 339 QLNEQISQLKKELTNSE--------------SENSEKQRELEEKQNEIEK----LKKENQSYKQEIKNLESQI 393
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
174-390 7.82e-04

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 41.20  E-value: 7.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 174 EALEGYKKKYEEELSlrpCAENEFVTLKKDVdtaflvkADLETNLEALEHEIeflkALFEEEISLLQSQISETSviVKMD 253
Cdd:COG1579  20 DRLEPRIKEIRKALK---KAKAELEALNKAL-------EALEIELEDLENQV----SQLESEIQEIRERIKRAE--EKLS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 254 NSRDLDvdgivaEIKA--QYDDIASRSKAEAEawyqcryEELRmtagnHSDNLRNRK-NEILEMNKLIQRLQQDIETVKA 330
Cdd:COG1579  84 AVKDER------ELRAlnIEIQIAKERINSLE-------DELA-----ELMEEIEKLeKEIEDLKERLERLEKNLAEAEA 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 331 qrcKLEGAIAQAEQQGEAALSdakcKLAGLEEALQKAkqdmacLLKEYQEVMNSKLGLDI 390
Cdd:COG1579 146 ---RLEEEVAEIREEGQELSS----KREELKEKLDPE------LLSEYERIRKNKKGVGV 192
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
94-400 1.19e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 41.67  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  94 DEKEQIKCLNNRFASFINK-VRFLEQKNKLLETKWNFMQQQRS----CQSNMEPLFEGYICALRRQLdcvSGDHGRLEAE 168
Cdd:COG0419 413 EELEKELEELERELEELEEeIKKLEEQINQLESKELMIAELAGagekCPVCGQELPEEHEKELLELY---ELELEELEEE 489
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 169 LcSLQEALEGYKKKYEE-ELSLRPCAENEFVTLKKDVdtafLVKADLETNLEALEHEIEFLKALFEEEISL-LQSQISET 246
Cdd:COG0419 490 L-SREKEEAELREEIEElEKELRELEEELIELLELEE----ALKEELEEKLEKLENLLEELEELKEKLQLQqLKEELRQL 564
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 247 SVIVK-----MDNSRDLDVDGI--------VAEIKAQYDDIASRSKAEAEAWYQCRYEELRMTAGNHSDNLRNRKNEILE 313
Cdd:COG0419 565 EDRLQelkelLEELRLLRTRKEeleelrerLKELKKKLKELEERLSQLEELLQSLELSEAENELEEAEEELESELEKLNL 644
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 314 MNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEAALSDAKCK--LAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIE 391
Cdd:COG0419 645 QAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLeeLEQLEEELEQLREELEELLKKLGEIEQLIEELESR 724

                ....*....
gi 57012336 392 IATYRRLLE 400
Cdd:COG0419 725 KAELEELKK 733
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
306-405 1.72e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    306 NRKNEILEMNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEAA----------LSDAKCKLAGLEEALQKAKQDMACLL 375
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeleelsrqISALRKDLARLEAEVEQLEERIAQLS 753
                           90       100       110
                   ....*....|....*....|....*....|.
gi 57012336    376 KEYQEVMNSKLGLDIEIATYR-RLLEGEEHR 405
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEeELAEAEAEI 784
SerS COG0172
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis];
303-371 2.23e-03

Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 223250 [Multi-domain]  Cd Length: 429  Bit Score: 40.27  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 303 NLRNRKN------EILEMNKLIQRLQQDIETVKAQRCKLEGAIAQAEQQGE-------AALSDAKCKLAGLEEALQKAKQ 369
Cdd:COG0172  17 KLKKRGGdaldvdKLLELDEERRKLLRELEELQAERNELSKEIGRALKRGEddaeeliAEVKELKEKLKELEAALDELEA 96

                ..
gi 57012336 370 DM 371
Cdd:COG0172  97 EL 98
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
92-380 3.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336   92 KRDEKEQIKCLNNRFASFINKVRFLEQKNK-LLETKW---------NFMQQQRSCQSNMEPLFEGY---ICALRRQLDCV 158
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKeLKELKEkaeeyiklsEFYEEYLDELREIEKRLSRLeeeINGIEERIKEL 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  159 SGDHGRLEaelcSLQEALEGYKKKYEEelsLRPCAEnEFVTLKKDVDTAFLVKADLE-TNLEALEHEIEFL---KALFEE 234
Cdd:PRK03918 334 EEKEERLE----ELKKKLKELEKRLEE---LEERHE-LYEEAKAKKEELERLKKRLTgLTPEKLEKELEELekaKEEIEE 405
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  235 EISLLQSQISETSVIVKMDNS----------------RDLDVD---GIVAEIKAQYDDIASRSK--AEAEAWYQCRYEEL 293
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKaieelkkakgkcpvcgRELTEEhrkELLEEYTAELKRIEKELKeiEEKERKLRKELREL 485
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336  294 RMTAGNHS---------DNLRNRKNEILEMN-KLIQRLQQDIETVKAQRCKLEGAIAQAEQQGEAaLSDAKCKLAGLEEA 363
Cdd:PRK03918 486 EKVLKKESeliklkelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKK 564
                        330
                 ....*....|....*..
gi 57012336  364 LQKAKQDMACLLKEYQE 380
Cdd:PRK03918 565 LDELEEELAELLKELEE 581
GumC COG3206
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ...
200-400 3.57e-03

Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225747 [Multi-domain]  Cd Length: 458  Bit Score: 39.73  E-value: 3.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 200 LKKDVDTAFLVKAdLETNLEALEHEIEFLkalfEEEISLLQ--SQISETSV--------IVKMDNSRDLDvDGIVAEIKA 269
Cdd:COG3206 173 LANALAQAYLADQ-LEAQLEAFRRASDSL----DERLEELRarLQEAEAQVedfraqhgLTDAARGQLLS-EQQLSALNT 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336 270 QYDDIASRSkAEAEAWYQCRYEEL-------RMTAGNHSDNLRNRKNEILEMNKLIQRLQQDIETVKAQRCKLEGAIAQA 342
Cdd:COG3206 247 QLQSARARL-AQAEARLASLLQLLplgreaaALREVLESPTIQDLRQQYAQVRQQIADLSTELGAKHPQLVALEAQLAEL 325
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57012336 343 EQQGEAALSDAKCKLAGLEEALQKAKQDMACLLKEYQEvMNSKLG--------LDIEIATYRRLLE 400
Cdd:COG3206 326 RQQIAAELRQILASLPNELALLEQQEAALEKELAQLKG-RLSKLPklqvqlreLEREAEAARSLYE 390
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
168-385 3.81e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.03  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    168 ELCSLQEALEGYKKKYEEELSLRPCAENEFVTLKKDVdtaflvkADLETNLEALEHEIEFLKALFEEEISLLQSqisets 247
Cdd:TIGR00606  710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEI-------PELRNKLQKVNRDIQRLKNDIEEQETLLGT------ 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    248 VIVKMDNSRDLDVD-GIVAEIKAQYDDIASRSKAEAEAWYQC----RYEELRMTAGNHSDNLRNRKNEILEMNKLIQRLQ 322
Cdd:TIGR00606  777 IMPEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQGSdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    323 QDIETVKA-------QRCKLEGAIAQAEQQGE-------------AALSDAKCKLAGLEEALQKakqdmacLLKEYQEVM 382
Cdd:TIGR00606  857 EQIQHLKSktnelksEKLQIGTNLQRRQQFEEqlvelstevqsliREIKDAKEQDSPLETFLEK-------DQQEKEELI 929

                   ...
gi 57012336    383 NSK 385
Cdd:TIGR00606  930 SSK 932
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
150-367 5.33e-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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 39.37  E-value: 5.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    150 ALRRQLDCVSGDHGRLEAELCSLQEALEGYKKKYEEELSLRPCAENEFVTLKKDVDtaflvkaDLETNLEALEHEIEFLk 229
Cdd:pfam01576  500 SLQEQLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRELE-------ALTQRLEEKAAAYDKL- 571
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57012336    230 alfEEEISLLQSQISEtsVIVKMDNSRDL---------DVDGIVAE---IKAQYDDiaSRSKAEAEAwyqcRYEELRMTA 297
Cdd:pfam01576  572 ---EKTKNRLQQELDD--LLVDLDHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEA----REKETKALS 640
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57012336    298 GNHS-DNLRNRKNEILEMNKLIQRLQQDIETVKAQRCK----LEGAIAQAEQQgeaaLSDAKCKLAGLEEALQKA 367
Cdd:pfam01576  641 LARAlEEALDAKEELERQNKQLRAEMEDLVSSKDDVGKnvheLERSKRALEQQ----VEEMKTQLEELEDELQAT 711
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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