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Conserved domains on  [gi|281363307|ref|NP_001163141|]
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centrosomin, isoform G [Drosophila melanogaster]

Protein Classification

Cnn_1N and PRK12704 domain-containing protein( domain architecture ID 10546816)

Cnn_1N and PRK12704 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 43-112 1.19e-18

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


:

Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 79.87  E-value: 1.19e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   43 RELEEQMSALRKENFNLKLRIYFLEEGQPGaRADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAAR 112
Cdd:pfam07989   1 REQEKQIDKLKKENFNLKLKIHFLEERLEK-LAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 29-342 3.03e-08

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 56.23  E-value: 3.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307    29 GGGNSPLPSQGRSVRELEE-QMSALRKENFNLKLRIYFLEEgqpgARADSSTESLSKQLIDAKIEIATLRKTVDvkmELL 107
Cdd:TIGR02169  657 GGSRAPRGGILFSRSEPAElQRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIE---QLE 729

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   108 KDAARAISHHEELQRKADIDSQAI-------------IDELQEQIHAYQMAES------GGQPVENIaktrkmlrlESEV 168
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIenvkselkelearIEELEEDLHKLEEALNdlearlSHSRIPEI---------QAEL 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   169 QRLEEELVNIEARnvaaRNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKE 248
Cdd:TIGR02169  801 SKLEEEVSRIEAR----LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   249 NQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIaklnAELETMRQQNVY 328
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELS 952

                          330
                   ....*....|....
gi 281363307   329 FRELSENLQQKEVR 342
Cdd:TIGR02169  953 LEDVQAELQRVEEE 966
 
Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 43-112 1.19e-18

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 79.87  E-value: 1.19e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   43 RELEEQMSALRKENFNLKLRIYFLEEGQPGaRADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAAR 112
Cdd:pfam07989   1 REQEKQIDKLKKENFNLKLKIHFLEERLEK-LAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 29-342 3.03e-08

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: 56.23  E-value: 3.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307    29 GGGNSPLPSQGRSVRELEE-QMSALRKENFNLKLRIYFLEEgqpgARADSSTESLSKQLIDAKIEIATLRKTVDvkmELL 107
Cdd:TIGR02169  657 GGSRAPRGGILFSRSEPAElQRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIE---QLE 729

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   108 KDAARAISHHEELQRKADIDSQAI-------------IDELQEQIHAYQMAES------GGQPVENIaktrkmlrlESEV 168
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIenvkselkelearIEELEEDLHKLEEALNdlearlSHSRIPEI---------QAEL 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   169 QRLEEELVNIEARnvaaRNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKE 248
Cdd:TIGR02169  801 SKLEEEVSRIEAR----LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   249 NQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIaklnAELETMRQQNVY 328
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELS 952

                          330
                   ....*....|....
gi 281363307   329 FRELSENLQQKEVR 342
Cdd:TIGR02169  953 LEDVQAELQRVEEE 966
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 80-346 4.50e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  80 ESLSKQLIDAKIEIATLRKTVDVKMELLKDAARAISHHEELQRKADIDSQAIIDELQEQIHAYQMAESGGQPVEN--IAK 157
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiARL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 158 TRKMLRLESEVQRLEEELVNIEARNVAARNELEfmlaERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDS 237
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 238 LKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNA 317
Cdd:COG1196  384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        250       260
                 ....*....|....*....|....*....
gi 281363307 318 ELETMRQQNVYFRELSENLQQKEVRQLDR 346
Cdd:COG1196  464 LLAELLEEAALLEAALAELLEELAEAAAR 492
46 PHA02562
endonuclease subunit; Provisional
 106-320 5.37e-07

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 51.94  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 106 LLKDAARAIshHEELQrkaDIDSQaiIDELQEQIHAYQ--MAESGGQPVENIAKTRKM--------LRLESEVQRLEEEL 175
Cdd:PHA02562 171 LNKDKIREL--NQQIQ---TLDMK--IDHIQQQIKTYNknIEEQRKKNGENIARKQNKydelveeaKTIKAEIEELTDEL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 176 VNIEarnvaarnelefmlaERLESLTACEGKIQELAIKNSELVERLEKE-------------TASAESSNEAIDSLKVEL 242
Cdd:PHA02562 244 LNLV---------------MDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptcTQQISEGPDRITKIKDKL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 243 EACRKENQDLVTSIRTLK---HDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAEL 319
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEeimDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL 388


                 .
gi 281363307 320 E 320
Cdd:PHA02562 389 D 389
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 30-340 3.36e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 3.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307    30 GGNSPLPSQGRSVRELEEQMSALRKENFNLKLRIYFLEEGQPGARADSSTESLSKQLIDA-KIEIATLRKTVDVKMELLK 108
Cdd:pfam15921  455 GKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAtNAEITKLRSRVDLKLQELQ 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   109 DAARAISHHEELQRKAD------IDSQAIIDELQEQIHayQMAESGGQpveniaKTRKMLRLESEVQRLEEElvnIEARN 182
Cdd:pfam15921  535 HLKNEGDHLRNVQTECEalklqmAEKDKVIEILRQQIE--NMTQLVGQ------HGRTAGAMQVEKAQLEKE---INDRR 603

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   183 VAARnELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHD 262
Cdd:pfam15921  604 LELQ-EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   263 MKRQVRSMKEAANTMDVQRQS----ILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFRELSENLQQ 338
Cdd:pfam15921  683 FRNKSEEMETTTNKLKMQLKSaqseLEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK 762


                   ..
gi 281363307   339 KE 340
Cdd:pfam15921  763 EK 764
 
Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 43-112 1.19e-18

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 79.87  E-value: 1.19e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   43 RELEEQMSALRKENFNLKLRIYFLEEGQPGaRADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAAR 112
Cdd:pfam07989   1 REQEKQIDKLKKENFNLKLKIHFLEERLEK-LAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 29-342 3.03e-08

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: 56.23  E-value: 3.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307    29 GGGNSPLPSQGRSVRELEE-QMSALRKENFNLKLRIYFLEEgqpgARADSSTESLSKQLIDAKIEIATLRKTVDvkmELL 107
Cdd:TIGR02169  657 GGSRAPRGGILFSRSEPAElQRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIE---QLE 729

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   108 KDAARAISHHEELQRKADIDSQAI-------------IDELQEQIHAYQMAES------GGQPVENIaktrkmlrlESEV 168
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIenvkselkelearIEELEEDLHKLEEALNdlearlSHSRIPEI---------QAEL 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   169 QRLEEELVNIEARnvaaRNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKE 248
Cdd:TIGR02169  801 SKLEEEVSRIEAR----LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   249 NQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIaklnAELETMRQQNVY 328
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELS 952

                          330
                   ....*....|....
gi 281363307   329 FRELSENLQQKEVR 342
Cdd:TIGR02169  953 LEDVQAELQRVEEE 966
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 80-346 4.50e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  80 ESLSKQLIDAKIEIATLRKTVDVKMELLKDAARAISHHEELQRKADIDSQAIIDELQEQIHAYQMAESGGQPVEN--IAK 157
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiARL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 158 TRKMLRLESEVQRLEEELVNIEARNVAARNELEfmlaERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDS 237
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 238 LKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNA 317
Cdd:COG1196  384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        250       260
                 ....*....|....*....|....*....
gi 281363307 318 ELETMRQQNVYFRELSENLQQKEVRQLDR 346
Cdd:COG1196  464 LLAELLEEAALLEAALAELLEELAEAAAR 492
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-349 4.61e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  42 VRELEEQMSALRKE--------NFNLKLRIYfleegqpgaradsSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAARA 113
Cdd:COG1196  195 LGELERQLEPLERQaekaeryrELKEELKEL-------------EAELLLLKLRELEAELEELEAELEELEAELEELEAE 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 114 ISHHEELQRKAdidsQAIIDELQEQIHAYQMAESggqpveniAKTRKMLRLESEVQRLEEELVNIEARNV---AARNELE 190
Cdd:COG1196  262 LAELEAELEEL----RLELEELELELEEAQAEEY--------ELLAELARLEQDIARLEERRRELEERLEeleEELAELE 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 191 FMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSM 270
Cdd:COG1196  330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281363307 271 KEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYfRELSENLQQKEVRQLDRGVA 349
Cdd:COG1196  410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 38-346 8.78e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 8.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307    38 QGRSVRELEEQMSALRKENFNLKlriyfleegQPGARADSSTESLSKQLIDAKIEIATLRKTVdvkmellkdaaRAISHH 117
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELE---------EELEQLRKELEELSRQISALRKDLARLEAEV-----------EQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   118 EELQRKADIDSQAIIDELQEQIHAYQMAEsggqpvenIAKTRKMLRLESEVQRLEEELVNIEARNVAARNELEFM---LA 194
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEEL--------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   195 ERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAA 274
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281363307   275 NTMDVQRQSILLLEATIKRKEKSCGSMQKNV----LNYEALIAKLNAELETMRQ---QNVYFRELSENLQQKEVRQLDR 346
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLegleVRIDNLQERLSEEYSLTLEeaeALENKIEDDEEEARRRLKRLEN 979
46 PHA02562
endonuclease subunit; Provisional
 106-320 5.37e-07

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 51.94  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 106 LLKDAARAIshHEELQrkaDIDSQaiIDELQEQIHAYQ--MAESGGQPVENIAKTRKM--------LRLESEVQRLEEEL 175
Cdd:PHA02562 171 LNKDKIREL--NQQIQ---TLDMK--IDHIQQQIKTYNknIEEQRKKNGENIARKQNKydelveeaKTIKAEIEELTDEL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 176 VNIEarnvaarnelefmlaERLESLTACEGKIQELAIKNSELVERLEKE-------------TASAESSNEAIDSLKVEL 242
Cdd:PHA02562 244 LNLV---------------MDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptcTQQISEGPDRITKIKDKL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 243 EACRKENQDLVTSIRTLK---HDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAEL 319
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEeimDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL 388


                 .
gi 281363307 320 E 320
Cdd:PHA02562 389 D 389
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 73-362 2.00e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307    73 ARADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAARAI---SHHEELQRKADIDS-QAIIDELQEQIHAYQmaesg 148
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlGEEEQLRVKEKIGElEAEIASLERSIAEKE----- 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   149 gqpveniaktRKMLRLESEVQRLEEELVNIEARNVAARNELEfMLAERLESLTAcegKIQELAIKNSELVERLEKETASA 228
Cdd:TIGR02169  315 ----------RELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTE---EYAELKEELEDLRAELEEVDKEF 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   229 ESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKscgSMQKNVLNY 308
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL---EIKKQEWKL 457

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 281363307   309 EALIAKLNAELETMRQQNVYFRELSENLQQKEvRQLDRGVAIVQPMRMTADAGR 362
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQ-RELAEAEAQARASEERVRGGR 510
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
40-342 1.49e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  40 RSVRELEEQMSALRKENFNLKLRIYFLEEGQPGAR-----ADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAA--- 111
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPvdl 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 112 -RAISHHEELQ-RKADI-----DSQAIIDELQEQI-HAYQMAESG-----GQPVENIAKTRKMLRLESEVQRLEEELVNI 178
Cdd:PRK02224 408 gNAEDFLEELReERDELrereaELEATLRTARERVeEAEALLEAGkcpecGQPVEGSPHVETIEEDRERVEELEAELEDL 487

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 179 EARnvaaRNELEFMLaERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSL---KVELEACRKENQDLVTS 255
Cdd:PRK02224 488 EEE----VEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELrerAAELEAEAEEKREAAAE 562

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 256 IRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEkscgsmqknvlNYEALIAKLNAELETMRQQNvyfRELSEN 335
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-----------DAEDEIERLREKREALAELN---DERRER 628


                 ....*..
gi 281363307 336 LQQKEVR 342
Cdd:PRK02224 629 LAEKRER 635
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
64-342 1.86e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   64 YFLEEGQPGARADSSTESLsKQLIDAKIEIATLRKtvdvKMELLKDAARaisHHEELQRKADidSQAIIDELQEQIHAYQ 143
Cdd:COG4913   216 YMLEEPDTFEAADALVEHF-DDLERAHEALEDARE----QIELLEPIRE---LAERYAAARE--RLAELEYLRAALRLWF 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  144 maesggqpveniaKTRKMLRLESEVQRLEEELVNIEARNVAARNELEFMLAERLESLTACEG----KIQELAIKNSELVE 219
Cdd:COG4913   286 -------------AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLER 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  220 RLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQsILLLEATIKRKEKScg 299
Cdd:COG4913   353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR-DLRRELRELEAEIA-- 429

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 281363307  300 SMQKNVLNYEaliaklnAELETMRqqnvyfRELSENLQQKEVR 342
Cdd:COG4913   430 SLERRKSNIP-------ARLLALR------DALAEALGLDEAE 459
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 30-340 3.36e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 3.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307    30 GGNSPLPSQGRSVRELEEQMSALRKENFNLKLRIYFLEEGQPGARADSSTESLSKQLIDA-KIEIATLRKTVDVKMELLK 108
Cdd:pfam15921  455 GKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAtNAEITKLRSRVDLKLQELQ 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   109 DAARAISHHEELQRKAD------IDSQAIIDELQEQIHayQMAESGGQpveniaKTRKMLRLESEVQRLEEElvnIEARN 182
Cdd:pfam15921  535 HLKNEGDHLRNVQTECEalklqmAEKDKVIEILRQQIE--NMTQLVGQ------HGRTAGAMQVEKAQLEKE---INDRR 603

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   183 VAARnELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHD 262
Cdd:pfam15921  604 LELQ-EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   263 MKRQVRSMKEAANTMDVQRQS----ILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFRELSENLQQ 338
Cdd:pfam15921  683 FRNKSEEMETTTNKLKMQLKSaqseLEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK 762


                   ..
gi 281363307   339 KE 340
Cdd:pfam15921  763 EK 764
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 33-274 5.96e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  33 SPLPSQGRSVRELEEQMSALRKENFNLKLRIyfleegqpgARADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAAR 112
Cdd:COG4942   13 LAAAAQADAAAEAEAELEQLQQEIAELEKEL---------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 113 AISHHEELQRKADIDSQAIIDELQEQIHAYQMAESGGQPV-----ENIAKTRKMLRLESEVQRLEEELVNIEARNVAARN 187
Cdd:COG4942   84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 188 ELEFMLAERLESLTAcegKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQV 267
Cdd:COG4942  164 ALRAELEAERAELEA---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240


                 ....*..
gi 281363307 268 RSMKEAA 274
Cdd:COG4942  241 ERTPAAG 247
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
158-346 6.09e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  158 TRKMLRLESEVQRLEEELVNIEARNVAARNELEfMLAERLESLTACEgKIQELAIKNSEL---VERLEKETASAESSNEA 234
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLA-EYSWDEIDVASAereIAELEAELERLDASSDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  235 IDSLKVELEACRKENQDLVTSIRTLKHDMKRqvrsmkeaantmdvqrqsillLEATIKRKEKSCGSMQKNVLNYEALIAK 314
Cdd:COG4913   687 LAALEEQLEELEAELEELEEELDELKGEIGR---------------------LEKELEQAEEELDELQDRLEAAEDLARL 745

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 281363307  315 -LNAELETMRQQNV---YFRELSENLQQkEVRQLDR 346
Cdd:COG4913   746 eLRALLEERFAAALgdaVERELRENLEE-RIDALRA 780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-351 1.14e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307    39 GRSVRELEEQMS------ALRKENFNLKLRIYFLEEGQPGARADSSTESLsKQLIDAKIEIATLRKTVDVKMELLKDAAR 112
Cdd:TIGR02168  199 ERQLKSLERQAEkaerykELKAELRELELALLVLRLEELREELEELQEEL-KEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   113 AISHHEELQRKADIDSQAIIDELQEQIHAYQmaESGGQPVENIAK-TRKMLRLESEVQRLEEELVNIEARNVAARNELEF 191
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILR--ERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELES 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   192 MLAErlesLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMK 271
Cdd:TIGR02168  356 LEAE----LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   272 EAAntMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQ--NVYFRELSENLQQKEVRQLDRGVA 349
Cdd:TIGR02168  432 EAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaQLQARLDSLERLQENLEGFSEGVK 509


                   ..
gi 281363307   350 IV 351
Cdd:TIGR02168  510 AL 511
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 80-256 1.34e-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: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  80 ESLSKQLIDAKIEIATLRKTVDVKMELLKDAARAISHHEElqrkaDIDS-QAIIDELQEQIhayqmaesggqpvENIAKT 158
Cdd:COG1579   27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-----EIEEvEARIKKYEEQL-------------GNVRNN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 159 RKMLRLESEVQRLEEELVNIEARnvaarnELEFMlaERLESLtacEGKIQELAIKNSELVERLEKETASAEssnEAIDSL 238
Cdd:COG1579   89 KEYEALQKEIESLKRRISDLEDE------ILELM--ERIEEL---EEELAELEAELAELEAELEEKKAELD---EELAEL 154

                        170
                 ....*....|....*...
gi 281363307 239 KVELEACRKENQDLVTSI 256
Cdd:COG1579  155 EAELEELEAEREELAAKI 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 155-348 1.82e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   155 IAKTRKMLRLESEVQRLEEELVNIEARNVAARNELEFM-----------------LAERLESLTACEGKIQELAIKNSEL 217
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELeeeleqlrkeleelsrqISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   218 VERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMK---------------------RQVRSMKEAANT 276
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrealdelraeltllneeaaNLRERLESLERR 832

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363307   277 MDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELET----MRQQNVYFRELSENLQQ--KEVRQLDRGV 348
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllneRASLEEALALLRSELEElsEELRELESKR 910
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 28-350 2.53e-04

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: 43.80  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307    28 PGGGNSPLPSQGRSVRELEEQMSALRKENFNLKLRIYFLEEGQpgARADSSTESLSKQLIDAKIEIATLRKTVDvkmeLL 107
Cdd:TIGR00618  523 PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM--QEIQQSFSILTQCDNRSKEDIPNLQNITV----RL 596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   108 KDAARAISHHEelqRKADIDSQAIIDELQEQIHAYQMAESGGQPVENIAKtrKMLRLESEVQRLEEELVNIEARnvAARN 187
Cdd:TIGR00618  597 QDLTEKLSEAE---DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL--KLTALHALQLTLTQERVREHAL--SIRV 669

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   188 ELEFMLAERLESLTACEGKIQELAIKNSELVERLEK----ETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDM 263
Cdd:TIGR00618  670 LPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLlrelETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM 749

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   264 KRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEA---LIAKLNAELETMRQQNVYFRELSENLQQKE 340
Cdd:TIGR00618  750 HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEdthLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829

                          330
                   ....*....|
gi 281363307   341 VRQLDRGVAI 350
Cdd:TIGR00618  830 EEQFLSRLEE 839
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
99-268 5.62e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  99 TVDVKMELLKD--------------AARAISHH----EELQRKA--DIDSQAIIDE----------LQEQIHAYQMAESG 148
Cdd:COG2433  316 SVEEKLHLAREygydndherdalaaALKAYDAYknkfERVEKKVppDVDRDEVKARvirglsieeaLEELIEKELPEEEP 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 149 GQPVENIA-------KTRKMLRLESEVQRLEEELVNIEARNVAARNELEfMLAERLESLtaceGKIQELAIKNSELVERL 221
Cdd:COG2433  396 EAEREKEHeerelteEEEEIRRLEEQVERLEAEVEELEAELEEKDERIE-RLERELSEA----RSEERREIRKDREISRL 470

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 281363307 222 EKEtasaessneaIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVR 268
Cdd:COG2433  471 DRE----------IERLERELEEERERIEELKRKLERLKELWKLEHS 507
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
72-266 6.75e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   72 GARADSSTESLSKQLIDAKIEIATLRKTV---DVKMELLKDAARAISHHEELQRkADIDSQAIIDELQEQIHAYQMAESG 148
Cdd:COG4913   605 GFDNRAKLAALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDAS 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  149 GQPVENIAKTRKmlRLESEVQRLEEELVNIEARNVAARNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASA 228
Cdd:COG4913   684 SDDLAALEEQLE--ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 281363307  229 ESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQ 266
Cdd:COG4913   762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 33-325 1.18e-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: 41.48  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  33 SPLPSQGRSVRELEEQMSALRKENFNLKLRIyflEEGQPGARADSSTESLSKQLidakieiatlrktvdvkmellkDAAR 112
Cdd:COG5185  268 EKLGENAESSKRLNENANNLIKQFENTKEKI---AEYTKSIDIKKATESLEEQL----------------------AAAE 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 113 AISHHEELQRKADIDsqaiIDELQEQIHayQMAESGGQPVENIAKTRKMLRLESEVQRLEEELVNIEARNVAARNELEfm 192
Cdd:COG5185  323 AEQELEESKRETETG----IQNLTAEIE--QGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLD-- 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 193 laerlESLTACEGKIQELAIK-------NSELVERLEKETASAESSNEAIDSLKVELEAC----RKENQDLVTSIRTLKH 261
Cdd:COG5185  395 -----EIPQNQRGYAQEILATledtlkaADRQIEELQRQIEQATSSNEEVSKLLNELISElnkvMREADEESQSRLEEAY 469

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281363307 262 D-MKRQVRSMKEAANTMDVQRQSILlleATIKRKEkscgsmqknvlnyEALIAKLNAELETMRQQ 325
Cdd:COG5185  470 DeINRSVRSKKEDLNEELTQIESRV---STLKATL-------------EKLRAKLERQLEGVRSK 518
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
132-318 1.48e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 132 IDELQEQIHAYQmaesggqpveniAKTRKMLRLESEVQRLEEELVNIEARNVAARNELEFMlaERLESLTACEGKIQELA 211
Cdd:COG4717   73 LKELEEELKEAE------------EKEEEYAELQEELEELEEELEELEAELEELREELEKL--EKLLQLLPLYQELEALE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 212 IKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSillLEATI 291
Cdd:COG4717  139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE---LEEEL 215

                        170       180
                 ....*....|....*....|....*..
gi 281363307 292 KRKEKSCGSMQKNVLNYEALIAKLNAE 318
Cdd:COG4717  216 EEAQEELEELEEELEQLENELEAAALE 242
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
42-340 1.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  42 VRELEEQMSALRKENFNLKLRIYFLEEGQPGARADSSTESLSKQLIDAKIEI----ATLRKTVDVKMELLKDAARAISHH 117
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIekrlSRLEEEINGIEERIKELEEKEERL 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 118 EELQRKADiDSQAIIDELQEQIHAYQMA------------ESGGQPVENIAKtrKMLRLESEVQRLEEELVNIEARnvaa 185
Cdd:PRK03918 341 EELKKKLK-ELEKRLEELEERHELYEEAkakkeelerlkkRLTGLTPEKLEK--ELEELEKAKEEIEEEISKITAR---- 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 186 RNELEFMLAER---LESLTACEGKI------------QELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQ 250
Cdd:PRK03918 414 IGELKKEIKELkkaIEELKKAKGKCpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 251 DLVTsirtlKHDMKRQVRSMKEAANTMDVQRqsillleatIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFR 330
Cdd:PRK03918 494 ELIK-----LKELAEQLKELEEKLKKYNLEE---------LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA 559

                        330
                 ....*....|
gi 281363307 331 ELSENLQQKE 340
Cdd:PRK03918 560 ELEKKLDELE 569
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
35-248 1.75e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   35 LPSQGRSVRELEEQMSALRKENFNLKLriyfLEEGQpgARADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAArai 114
Cdd:COG4913   663 VASAEREIAELEAELERLDASSDDLAA----LEEQL--EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ--- 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  115 shhEELQRKADIDSQAIIDELQEQIHAYQMAESGGQPVENIAKTRKmlRLESEVQRLEEELVNIEArnvAARNELEFMLA 194
Cdd:COG4913   734 ---DRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID--ALRARLNRAEEELERAMR---AFNREWPAETA 805

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281363307  195 ERLESLTACEGKIQELA-IKNSELVERLEK-ETASAESSNEAIDSLKVELEACRKE 248
Cdd:COG4913   806 DLDADLESLPEYLALLDrLEEDGLPEYEERfKELLNENSIEFVADLLSKLRRAIRE 861
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
153-342 2.28e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 153 ENIAKTRKMLRLESEvqRLEEELvniearnvAARNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKetasAESSN 232
Cdd:PRK03918 165 KNLGEVIKEIKRRIE--RLEKFI--------KRTENIEELIKEKEKELEEVLREINEISSELPELREELEK----LEKEV 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 233 EAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEaTIKRKEKSCGSMQKNVLNYEALI 312
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309

                        170       180       190
                 ....*....|....*....|....*....|
gi 281363307 313 AKLNAELETMRQQNVYFRELSENLQQKEVR 342
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEER 339
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 84-276 2.88e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 40.22  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  84 KQLIDAKIEIATLRKTVDVKMELLKDAAraisHHEELQRKADIDsqaiiDELqeqihayqmaesggqpVENIAKTRKMLR 163
Cdd:PLN03229 560 KAEINKKFKEVMDRPEIKEKMEALKAEV----ASSGASSGDELD-----DDL----------------KEKVEKMKKEIE 614

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 164 LE--SEVQRLEEELVNIEARNVAARNELEFM-LAERLESLTACEGKIQELAIKNSEL---VERLEKETASAESSNEAIDS 237
Cdd:PLN03229 615 LElaGVLKSMGLEVIGVTKKNKDTAEQTPPPnLQEKIESLNEEINKKIERVIRSSDLkskIELLKLEVAKASKTPDVTEK 694

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 281363307 238 LKVE-LEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANT 276
Cdd:PLN03229 695 EKIEaLEQQIKQKIAEALNSSELKEKFEELEAELAAARET 734
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
42-310 3.13e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  42 VRELEEQMSALRKENFNLKLRIYFLEEGQPGARADSSTESLSKQLIDAKIEiaTLRKTVDVKMELLKDAARAISHHEE-- 119
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEea 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 120 ---LQRKADIDSQAiiDELQEQIHAyqmAESGGQPVENIAKTRkmlrlESEVQRLEEELVNIEAR---NVAARNELEFML 193
Cdd:PRK02224 345 eslREDADDLEERA--EELREEAAE---LESELEEAREAVEDR-----REEIEELEEEIEELRERfgdAPVDLGNAEDFL 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 194 AERLESLTACEGKIQELAIKNSELVERLEKETA---------------------SAESSNEAIDSLKVELEACRKENQDL 252
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEV 494

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 281363307 253 VTSIRTLKhDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEA 310
Cdd:PRK02224 495 EERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
80-250 4.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  80 ESLSKQLIDAKIEIATLRKTVDvKMELLKDAARAISHHEELQRK-ADIDSQaiIDELQEQIHAYQmaesggqpveniakt 158
Cdd:COG4717   98 EELEEELEELEAELEELREELE-KLEKLLQLLPLYQELEALEAElAELPER--LEELEERLEELR--------------- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 159 rkmlRLESEVQRLEEELVNIEARNVAARNELEFMLAERLESLTAcegKIQELAIKNSELVERLEKETASAESSNEAIDSL 238
Cdd:COG4717  160 ----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE---ELEELQQRLAELEEELEEAQEELEELEEELEQL 232

                        170
                 ....*....|..
gi 281363307 239 KVELEACRKENQ 250
Cdd:COG4717  233 ENELEAAALEER 244
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 128-372 5.07e-03

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: 38.98  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 128 SQAIIDELQEQIHAYQmaesggqpvENIAKTRKML-RLESEVQRLEEELVNIEARNVAARNELEfMLAERLESLtacEGK 206
Cdd:COG4942   18 QADAAAEAEAELEQLQ---------QEIAELEKELaALKKEEKALLKQLAALERRIAALARRIR-ALEQELAAL---EAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 207 IQELAIKNSELVERLEK------ETASAESSNEAIDSLKVELEAcrKENQDLVTSIRTLKH---DMKRQVRSMKEAANTM 277
Cdd:COG4942   85 LAELEKEIAELRAELEAqkeelaELLRALYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYlapARREQAEELRADLAEL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307 278 DVQRQSIL----LLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFRELSENLQQ---KEVRQLDRGVAI 350
Cdd:COG4942  163 AALRAELEaeraELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliaRLEAEAAAAAER 242

                        250       260
                 ....*....|....*....|...
gi 281363307 351 VQPMRMTADAGRFVW-QSGTIVA 372
Cdd:COG4942  243 TPAAGFAALKGKLPWpVSGRVVR 265
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 158-288 5.11e-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: 39.39  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   158 TRKMLRLESEVQRLEEElvniearnvaaRNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDS 237
Cdd:pfam01576  481 TRQKLNLSTRLRQLEDE-----------RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR 549

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 281363307   238 LKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLE 288
Cdd:pfam01576  550 LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLE 600
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 40-344 5.55e-03

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: 39.34  E-value: 5.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   40 RSVRELEEQMSALRKENFNLKLRIYFLEegqpgaradSSTESLSKQLIDAKIEIATLRKTVdvkMELLKDAARAISHHEE 119
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREIVLKEENSSLT---------SSARQLEKARRELEQELAQYLKKI---EDLNKKLKRHKALVRR 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  120 LQRKADIDSQAIiDELQEQIHAYQ----MAESGGQpveniaKTRKMLRLESEVQRLEEELVNIEARnvaaRNELEFMLAE 195
Cdd:pfam05557 344 LQRRVLLLTKER-DGYRAILESYDkeltMSNYSPQ------LLERIEEAEDMTQKMQAHNEEMEAQ----LSVAEEELGG 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  196 RLESLTACEGKIQELaiknselveRLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQ-VRSMKEAA 274
Cdd:pfam05557 413 YKQQAQTLERELQAL---------RQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRcLQGDYDPK 483

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  275 NTMDVQRQSILLLEATIKRKEKScGSMQKNVLNYEALIAKLNAELETMRQQNvyfrELSENLQQKEVRQL 344
Cdd:pfam05557 484 KTKVLHLSMNPAAEAYQQRKNQL-EKLQAEIERLKRLLKKLEDDLEQVLRLP----ETTSTMNFKEVLDL 548
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 43-339 5.64e-03

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: 39.23  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307   43 RELEEQMSALR---KENFNLKLRIYFLEegqpgaradSSTESLSKQLIDAKieiaTLRKTVDVKMELLKDAARAISHHEE 119
Cdd:TIGR04523 363 RELEEKQNEIEklkKENQSYKQEIKNLE---------SQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEKEIE 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  120 LQRKADIDSQAIIDELQEQIHAYQMAesggqpVENIAKTRKMLR-----LESEVQRLEEELVNIEARNVAARNELEFMLA 194
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELI------IKNLDNTRESLEtqlkvLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363307  195 ERLESltacEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEacrKENQDLVTS-IRTLKHDMKRQVRSMKEA 273
Cdd:TIGR04523 504 EKKEL----EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN---KDDFELKKEnLEKEIDEKNKEIEELKQT 576

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281363307  274 ANTMDV-QRQsillLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFRELSENLQQK 339
Cdd:TIGR04523 577 QKSLKKkQEE----KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
 
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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