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Conserved domains on  [gi|17865632|ref|NP_065800|]
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microtubule-associated tumor suppressor 1 isoform 5 [Homo sapiens]

Protein Classification

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

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-381 2.40e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.77  E-value: 2.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632     85 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 160
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    161 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEAS--LSE 238
Cdd:TIGR02168  751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    239 IKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSE--------NDALNEKLKSEEQKRRAREKANLKNPQIMYLEQ 304
Cdd:TIGR02168  829 LERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRELES 908

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865632    305 ELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 381
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-381 2.40e-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: 62.77  E-value: 2.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632     85 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 160
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    161 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEAS--LSE 238
Cdd:TIGR02168  751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    239 IKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSE--------NDALNEKLKSEEQKRRAREKANLKNPQIMYLEQ 304
Cdd:TIGR02168  829 LERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRELES 908

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865632    305 ELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 381
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 112-398 1.58e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 112 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFY-----------TRE 180
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarleqDIA 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 181 YEKLRdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 260
Cdd:COG1196 306 RLEER---RRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 261 LEKQINDLKSENDALNEKLKSEE----QKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 336
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865632 337 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLW 398
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
PRK09039 PRK09039
peptidoglycan -binding protein;
200-350 9.67e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.27  E-value: 9.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  200 QEQFDNLNA--AHETSKLEIEASHSEKLELLKKAYEASLSEIkkghEIEKKSLEDLLSEkqesLEKQINDLKSENDALNE 277
Cdd:PRK09039  52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLSAA----EAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865632  278 KLKSEEQ-KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM-EKLvdnNTALVDK---LKRFQQE 350
Cdd:PRK09039 124 ELDSEKQvSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRSE 198
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 107-425 4.10e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   107 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYE---AFVQQHQAEKTERENRL----KEFYTR 179
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELerirQEERKR 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   180 EYEKLRD-------TYIEEAEKYKMQLQEQFDNLNAAHETSKLE--IEASHSEKLELLKKAYEASLSEIKKGHEIEKKSL 250
Cdd:pfam17380 361 ELERIRQeeiameiSRMRELERLQMERQQKNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   251 ED-----LLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-AVLEIKNEKlhqqd 324
Cdd:pfam17380 441 EEerareMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEERKR----- 515

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   325 iKLMKMEkLVDNNTALVDKLKRFQQENEELKAR-MDKHMAISRQL--STEQAVLQESLEKESKVNKRLsMENEELLWKLh 401
Cdd:pfam17380 516 -KLLEKE-MEERQKAIYEEERRREAEEERRKQQeMEERRRIQEQMrkATEERSRLEAMEREREMMRQI-VESEKARAEY- 591

                         330       340
                  ....*....|....*....|....
gi 17865632   402 ngdlcsPKRSPTSSAIPLQSPRNS 425
Cdd:pfam17380 592 ------EATTPITTIKPIYRPRIS 609
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 189-349 6.68e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 44.67  E-value: 6.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 189 IEEAEKYKMQLQEQFDNLNAAHETSKleieaSHSEKLELLKKAYEASLSeiKKGHEIEKKSLEDLLSEKQESLEKQINDL 268
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKL 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 269 KSENDALNEKLKSEEQKRRAREK---------ANLKN------PQIMYLEQ----------ELESLKAVLEIKNEKLHQQ 323
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAALRliadltaadTDLDNllaligPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAA 279

                       170       180
                ....*....|....*....|....*.
gi 17865632 324 DIKLMKMEKLVDNNTALVDKLKRFQQ 349
Cdd:cd22656 280 ILAKLELEKAIEKWNELAEKADKFRQ 305
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 178-316 1.07e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    178 TREYEKLRDtYIEEAEKYKMQLQEQFDNLNaahetSKLEIEASHSEKLELLK----KAYEASLSEIKKGHEIEKKSLEDL 253
Cdd:smart00787 157 KEDYKLLMK-ELELLNSIKPKLRDRKDALE-----EELRQLKQLEDELEDCDptelDRAKEKLKKLLQEIMIKVKKLEEL 230

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865632    254 LSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpQIMYLEQELESLKAVLEIK 316
Cdd:smart00787 231 EEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-381 2.40e-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: 62.77  E-value: 2.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632     85 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 160
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    161 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEAS--LSE 238
Cdd:TIGR02168  751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    239 IKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSE--------NDALNEKLKSEEQKRRAREKANLKNPQIMYLEQ 304
Cdd:TIGR02168  829 LERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRELES 908

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865632    305 ELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 381
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 112-398 1.58e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 112 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFY-----------TRE 180
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarleqDIA 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 181 YEKLRdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 260
Cdd:COG1196 306 RLEER---RRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 261 LEKQINDLKSENDALNEKLKSEE----QKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 336
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865632 337 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLW 398
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-384 1.60e-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: 56.99  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    109 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQ---------QHQAEKTERENRLKEFYTR 179
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrleqqkQILRERLANLERQLEELEA 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    180 EYEKL---RDTYIEEA---EKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLE-D 252
Cdd:TIGR02168  324 QLEELeskLDELAEELaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEiE 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    253 LLSEKQESLEKQINDLKSENDALNEKLkSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEK 332
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKL-EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17865632    333 LVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESK 384
Cdd:TIGR02168  483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-396 2.42e-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: 56.60  E-value: 2.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    115 EALKQHKTLSQELVNLRGELVTASTtcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEfytreyeklrdtyIEEAEK 194
Cdd:TIGR02168  210 EKAERYKELKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEK-------------LEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    195 YKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEK-KSLEDLLSEKQESLEKQINDLKSEND 273
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEElESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    274 ALNEKLKSEEQKRRAREKANLKnpqimyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVdnnTALVDKLKRFQQENEE 353
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEE------LEEQLETLRSKVAQLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEE 425

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 17865632    354 LKARMDKH--MAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 396
Cdd:TIGR02168  426 LLKKLEEAelKELQAELEELEEELEELQEELERLEEALEELREEL 470
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-397 2.31e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 2.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 160 QQHQAEKTERENRLK----EFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEAS 235
Cdd:COG1196 216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 236 LSEIKKGHEIEkksledLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVLEI 315
Cdd:COG1196 295 AELARLEQDIA------RLEERRRELEERLEELEEELAELEEELEELEEELEELEE------ELEEAEEELEEAEAELAE 362

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 316 KNEKLHQQDIKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSM 391
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAeellEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442


                ....*.
gi 17865632 392 ENEELL 397
Cdd:COG1196 443 ALEEAA 448
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 142-396 3.37e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 3.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    142 EKLEKARNELQTVYE--AFVQQHQAEKTERENRLKEfytreyEKlrdtyiEEAEKYKMQLQEqfdnlnaahetsKLEIEA 219
Cdd:TIGR02169  170 RKKEKALEELEEVEEniERLDLIIDEKRQQLERLRR------ER------EKAERYQALLKE------------KREYEG 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    220 ShseKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKAnlknpQI 299
Cdd:TIGR02169  226 Y---ELLKEKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE-----KI 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    300 MYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQE--------NEELKARMDKHMAISRQLSTE 371
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEELEDLRAELEEV 376

                          250       260
                   ....*....|....*....|....*
gi 17865632    372 QAVLQESLEKESKVNKRLSMENEEL 396
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREI 401
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 100-325 9.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 9.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 100 EALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQaektERENRLKEFYTR 179
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA----EAEEELEELAEE 387

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 180 EYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 259
Cdd:COG1196 388 LLEALRA--AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----AAEEEAELEEEEEA 460

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865632 260 SLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDI 325
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 106-308 3.36e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 3.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 106 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLkefytREYEKLR 185
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE-----AELAEAE 378

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 186 DTYIEEAEKYKMQLQEQFDNLNA-AHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQ 264
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17865632 265 INDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELES 308
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
145-393 5.28e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 5.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 145 EKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKL-----EIEA 219
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKE-LEEAEAALEEFRQKNGLVDLSEEAKLLlqqlsELES 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 220 SHSEkLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ-ESLEKQINDLKSENDALNEKLKSeeqkrrarekanlKNPQ 298
Cdd:COG3206 227 QLAE-ARAELAEAEARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARYTP-------------NHPD 292

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 299 IMYLEQELESLKAvlEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQES 378
Cdd:COG3206 293 VIALRAQIAALRA--QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370

                       250
                ....*....|....*..
gi 17865632 379 LEK--ESKVNKRLSMEN 393
Cdd:COG3206 371 LQRleEARLAEALTVGN 387
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 107-396 8.65e-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: 48.14  E-value: 8.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    107 QHLLSEREEALKqHKTLSQELVNLRGELVTAsttceKLEKARNELQTVyEAFVQQHQAEKTERENRLKEFyTREYEKLRD 186
Cdd:TIGR02169  201 ERLRREREKAER-YQALLKEKREYEGYELLK-----EKEALERQKEAI-ERQLASLEEELEKLTEEISEL-EKRLEEIEQ 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    187 TYIEEAEKYK-------MQLQEQFDNLNAAHETSKLEIEASHS--EKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEK 257
Cdd:TIGR02169  273 LLEELNKKIKdlgeeeqLRVKEKIGELEAEIASLERSIAEKERelEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    258 qESLEKQINDLKSENDALNEKLKSEEQK-RRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVdn 336
Cdd:TIGR02169  353 -DKLTEEYAELKEELEDLRAELEEVDKEfAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI-- 429

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865632    337 nTALVDKLKRFQQENEELKARMDKH----MAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 396
Cdd:TIGR02169  430 -AGIEAKINELEEEKEDKALEIKKQewklEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
PRK09039 PRK09039
peptidoglycan -binding protein;
200-350 9.67e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.27  E-value: 9.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  200 QEQFDNLNA--AHETSKLEIEASHSEKLELLKKAYEASLSEIkkghEIEKKSLEDLLSEkqesLEKQINDLKSENDALNE 277
Cdd:PRK09039  52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLSAA----EAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865632  278 KLKSEEQ-KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM-EKLvdnNTALVDK---LKRFQQE 350
Cdd:PRK09039 124 ELDSEKQvSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRSE 198
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 142-394 1.29e-05

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: 47.66  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    142 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHetSKLEIEASH 221
Cdd:TIGR00618  127 ETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMN--LFPLDQYTQLALMEFAKKKSLH--GKAELLTLR 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    222 SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKqindLKSENDALNEKLKSEEQKRRAREKanlknpqimy 301
Cdd:TIGR00618  203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----LTQKREAQEEQLKKQQLLKQLRAR---------- 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    302 lEQELESLKAVLEIKNEKLHQQdiklMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 381
Cdd:TIGR00618  269 -IEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343

                          250
                   ....*....|...
gi 17865632    382 ESKVNKRLSMENE 394
Cdd:TIGR00618  344 RRLLQTLHSQEIH 356
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 257-382 1.75e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 257 KQESLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMK------ 329
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDAlQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 330 ---------------------------MEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKE 382
Cdd:COG3883  97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 82-354 2.25e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632     82 SGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEK---ARNELQTVYEAF 158
Cdd:TIGR02169  666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    159 VQQHQAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSE 238
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEAR---------IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    239 IKKGHEIEKKSLEDLLSEKQES------LEKQINDLKSENDALN---EKLKSEEQKRRA-------------REKANLKN 296
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELqeqridLKEQIKSIEKEIENLNgkkEELEEELEELEAalrdlesrlgdlkKERDELEA 896

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17865632    297 pQIMYLEQELESLKAVLEIKNEKLHQQDIKLmkmEKLVDNNTALVDKLKRFQQENEEL 354
Cdd:TIGR02169  897 -QLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELSEIEDPKGEDEEIPEEE 950
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 107-425 4.10e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   107 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYE---AFVQQHQAEKTERENRL----KEFYTR 179
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELerirQEERKR 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   180 EYEKLRD-------TYIEEAEKYKMQLQEQFDNLNAAHETSKLE--IEASHSEKLELLKKAYEASLSEIKKGHEIEKKSL 250
Cdd:pfam17380 361 ELERIRQeeiameiSRMRELERLQMERQQKNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   251 ED-----LLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-AVLEIKNEKlhqqd 324
Cdd:pfam17380 441 EEerareMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEERKR----- 515

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   325 iKLMKMEkLVDNNTALVDKLKRFQQENEELKAR-MDKHMAISRQL--STEQAVLQESLEKESKVNKRLsMENEELLWKLh 401
Cdd:pfam17380 516 -KLLEKE-MEERQKAIYEEERRREAEEERRKQQeMEERRRIQEQMrkATEERSRLEAMEREREMMRQI-VESEKARAEY- 591

                         330       340
                  ....*....|....*....|....
gi 17865632   402 ngdlcsPKRSPTSSAIPLQSPRNS 425
Cdd:pfam17380 592 ------EATTPITTIKPIYRPRIS 609
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 189-349 6.68e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 44.67  E-value: 6.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 189 IEEAEKYKMQLQEQFDNLNAAHETSKleieaSHSEKLELLKKAYEASLSeiKKGHEIEKKSLEDLLSEKQESLEKQINDL 268
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKL 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 269 KSENDALNEKLKSEEQKRRAREK---------ANLKN------PQIMYLEQ----------ELESLKAVLEIKNEKLHQQ 323
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAALRliadltaadTDLDNllaligPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAA 279

                       170       180
                ....*....|....*....|....*.
gi 17865632 324 DIKLMKMEKLVDNNTALVDKLKRFQQ 349
Cdd:cd22656 280 ILAKLELEKAIEKWNELAEKADKFRQ 305
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 81-292 9.95e-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: 44.37  E-value: 9.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  81 QSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQ 160
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 161 QHQAEKTERENRLKEFYT---REYEKL------------RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKL 225
Cdd:COG4942  98 ELEAQKEELAELLRALYRlgrQPPLALllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865632 226 ELLK--KAYEASLSEIKKgheiEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 292
Cdd:COG4942 178 ALLAelEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 70-287 2.20e-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: 43.89  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632     70 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 149
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    150 ELQTVYEAF---VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 226
Cdd:TIGR02168  863 ELEELIEELeseLEALLNERASLEEALALL-RSELEELSEE-LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865632    227 LLKKA---YEASLSEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSEN-DALNEklkSEEQKRR 287
Cdd:TIGR02168  941 LQERLseeYSLTLEEAEA-LENKIEDDEEEARRRLKRLENKIKELGPVNlAAIEE---YEELKER 1001
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 199-288 2.25e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.38  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  199 LQE----QFDNLNAAHETSKLEIEASH----SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESL---EKQIND 267
Cdd:PRK05771  25 LHElgvvHIEDLKEELSNERLRKLRSLltklSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELekiEKEIKE 104

                         90       100
                 ....*....|....*....|.
gi 17865632  268 LKSENDALNEKLKSEEQKRRA 288
Cdd:PRK05771 105 LEEEISELENEIKELEQEIER 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 190-395 3.63e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 190 EEAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEdLLSEKQESLEKQINDLK 269
Cdd:COG1196 210 EKAERYR-ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE-ELRLELEELELELEEAQ 287

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 270 SENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVLEIKNEKL--HQQDIKLMKMEKLVDNNTALVDKLKRF 347
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEE------RRRELEERLEELEEELAELEEELeeLEEELEELEEELEEAEEELEEAEAELA 361

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17865632 348 QQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEE 395
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 189-431 3.92e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 3.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 189 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAYEASLSEIKKgheiekksledlLSEKQESLEKQINDL 268
Cdd:COG4942  22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-LAALERRIAALARRIRA------------LEQELAALEAELAEL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 269 KSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE------------QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 336
Cdd:COG4942  89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAE 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 337 NTALVDKLKRFQQENEE----LKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHNGDLCSPKRSP 412
Cdd:COG4942 169 LEAERAELEALLAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAEEL----EALIARLEAEAAAAAERTP 244

                       250
                ....*....|....*....
gi 17865632 413 TSSAiplqsPRNSGSFPSP 431
Cdd:COG4942 245 AAGF-----AALKGKLPWP 258
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 66-388 4.52e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632     66 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKT-LSQELVNLRGELVTASTTCEKL 144
Cdd:pfam02463  690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEKEEEKSEL 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    145 EKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREyeklrdtyIEEAEKYKMQLQEQFDNL-NAAHETSKLEIEASHSE 223
Cdd:pfam02463  770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA--------LEEELKEEAELLEEEQLLiEQEEKIKEEELEELALE 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    224 KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQinDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 303
Cdd:pfam02463  842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI 919

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    304 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKES 383
Cdd:pfam02463  920 EERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999


                   ....*
gi 17865632    384 KVNKR 388
Cdd:pfam02463 1000 LEEEK 1004
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 178-316 1.07e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    178 TREYEKLRDtYIEEAEKYKMQLQEQFDNLNaahetSKLEIEASHSEKLELLK----KAYEASLSEIKKGHEIEKKSLEDL 253
Cdd:smart00787 157 KEDYKLLMK-ELELLNSIKPKLRDRKDALE-----EELRQLKQLEDELEDCDptelDRAKEKLKKLLQEIMIKVKKLEEL 230

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865632    254 LSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpQIMYLEQELESLKAVLEIK 316
Cdd:smart00787 231 EEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
PRK12704 PRK12704
phosphodiesterase; Provisional
 245-384 1.33e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  245 IEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE------EQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNE 318
Cdd:PRK12704  24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEakeeihKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865632  319 KLHQQDIKLMKMEKLVDNNTALVDKLkrfQQENEELKARMDKHMAISRQLSTEQA--VLQESLEKESK 384
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERISGLTAEEAkeILLEKVEEEAR 168
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
114-286 1.41e-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: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  114 EEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKefytREyeklrdtyIEEAE 193
Cdd:COG4913  284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----RE--------IERLE 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  194 KYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEikkgheiekKSLEDLLSEKQESLEKQINDLKSEND 273
Cdd:COG4913  352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL---------EEELEALEEALAEAEAALRDLRRELR 422

                        170
                 ....*....|...
gi 17865632  274 ALNEKLKSEEQKR 286
Cdd:COG4913  423 ELEAEIASLERRK 435
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 214-323 1.43e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 214 KLEIEASHSEKLELlkkayEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE----EQKRRAR 289
Cdd:COG0542 403 RMEIDSKPEELDEL-----ERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkeliEEIQELK 477

                        90       100       110
                ....*....|....*....|....*....|....
gi 17865632 290 EKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQ 323
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREE 511
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 112-392 1.54e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   112 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA---EKTERENRLKEF---------YTR 179
Cdd:pfam07888  67 DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAllaQRAAHEARIRELeediktltqRVL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   180 EYEKLRDTYIEEAEKYKMQLQEQfdnlNAAHETSKLEIEASHSEKLELLKKAYEAslseikKGHEIEKKSLEDLLSEKQE 259
Cdd:pfam07888 147 ERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQEL------RNSLAQRDTQVLQLQDTIT 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   260 SLEKQINDlKSENDALNEKLKseEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDNNT 338
Cdd:pfam07888 217 TLTQKLTT-AHRKEAENEALL--EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQLADASL 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 17865632   339 ALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSME 392
Cdd:pfam07888 294 ALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
PRK12704 PRK12704
phosphodiesterase; Provisional
 179-373 2.05e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  179 REYEKLRDTYIEEAEKykmqlqeqfdnlNAAHETSKLEIEAShsEKLELLKKAYEASLSEIKKghEIEKksLEDLLSEKQ 258
Cdd:PRK12704  34 KEAEEEAKRILEEAKK------------EAEAIKKEALLEAK--EEIHKLRNEFEKELRERRN--ELQK--LEKRLLQKE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  259 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESLKAVLEIKNEK---LHQQDIKLMKMEKLVD 335
Cdd:PRK12704  96 ENLDRKLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 17865632  336 NNTAlvDKLKRFQQENEELKARMDKH------MAISRqLSTEQA 373
Cdd:PRK12704 166 EARH--EAAVLIKEIEEEAKEEADKKakeilaQAIQR-CAADHV 206
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 165-285 2.70e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  165 EKTERENRLKEFYTREYEKLRdtyiEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEI----- 239
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALL----KEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17865632  240 KKGHEIEKKSLED---LLSEKQESLEKQINDLKSENDALNE----KLKSEEQK 285
Cdd:PRK00409 599 GGYASVKAHELIEarkRLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 185-396 2.81e-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: 40.04  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    185 RDTYIEEA---EKYKMQLQEQFDNLNAAHET---------------SKLEIEASHSEKLellkKAYEASLSEIKKG-HEI 245
Cdd:TIGR02168  157 RRAIFEEAagiSKYKERRKETERKLERTRENldrledilnelerqlKSLERQAEKAERY----KELKAELRELELAlLVL 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    246 EKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESL-KAVLEIKNEklhQQD 324
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----------LEEEIEELqKELYALANE---ISR 299

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865632    325 IKLMKMEkLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 396
Cdd:TIGR02168  300 LEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 114-396 2.82e-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: 40.11  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   114 EEALKQHKTLSQELVNLRGELVTASTTC-EKLEKARNELQtvYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtYIEEA 192
Cdd:pfam05557  44 DRESDRNQELQKRIRLLEKREAEAEEALrEQAELNRLKKK--YLEALNKKLNEKESQLADAREVISCLKNELSE-LRRQI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   193 EKYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLELLKKAYEASLSEIKKgHEIEKKSLEDLLsEKQESLEKQINDLKSEN 272
Cdd:pfam05557 121 QRAELELQSTNSELEELQE--RLDLLKAKASEAEQLRQNLEKQQSSLAE-AEQRIKELEFEI-QSQEQDSEIVKNSKSEL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   273 DALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-------------AVLEIKNEKLHQqdiKLMKMEKLVDNNT- 338
Cdd:pfam05557 197 ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklereekyreeaATLELEKEKLEQ---ELQSWVKLAQDTGl 273

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865632   339 ------ALVDKLKRFQQENEELKARMD------KHMAIS-RQLSTEQAVLQESLEKESKVNKRLSMENEEL 396
Cdd:pfam05557 274 nlrspeDLSRRIEQLQQREIVLKEENSsltssaRQLEKArRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
PTZ00121 PTZ00121
MAEBL; Provisional
 145-291 3.09e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   145 EKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEiEASHSEK 224
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEE-RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEE 1300

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865632   225 L----ELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREK 291
Cdd:PTZ00121 1301 KkkadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 106-259 3.63e-03

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: 38.75  E-value: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 106 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY---EAFVQQHQAEKTERENRLKEFYT-REY 181
Cdd:COG1579  12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNVRNnKEY 91

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865632 182 EKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAsHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQE 259
Cdd:COG1579  92 EALQKE-IESLKRRISDLEDEILELMERIEELEEELAE-LEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
PTZ00121 PTZ00121
MAEBL; Provisional
 110-326 3.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   110 LSEREEALKQHKTLSQELVNLRGElvTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYI 189
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   190 EEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKlELLKKAYEA-SLSEIKKGHEIEKKSLEDLLSEKQESLEKqINDL 268
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE-ALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIK-AEEA 1735

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17865632   269 KSENDalNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK 326
Cdd:PTZ00121 1736 KKEAE--EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-359 4.29e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  121 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFvqQHQAEKTERENRLKEfYTREYEKLRDTY--IEEAEKYKMQ 198
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVAS-AEREIAELEAELerLDASSDDLAA 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  199 LQEQFDNLNAAHETSKLEIEASHSEK---------LELLKKAYEASLSEIKKGHEIEKKSL--EDLLSEKQESLEKQI-N 266
Cdd:COG4913  690 LEEQLEELEAELEELEEELDELKGEIgrlekeleqAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVERELrE 769

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  267 DLKSENDALNEKLKSEEQK-RRAREKANLKNPQIMY-LEQELESLKAVLE----IKNEKL--HQQDIKLMKMEKLVDNNT 338
Cdd:COG4913  770 NLEERIDALRARLNRAEEElERAMRAFNREWPAETAdLDADLESLPEYLAlldrLEEDGLpeYEERFKELLNENSIEFVA 849

                        250       260
                 ....*....|....*....|.
gi 17865632  339 ALVDKLKRfqqENEELKARMD 359
Cdd:COG4913  850 DLLSKLRR---AIREIKERID 867
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 189-332 6.51e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 6.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  189 IEEAEKYKMQLQEQFDNLnaahetskleIEASHSEKLELLKKAYEASlsEIKKGHEIEKKSLEDLLSEKQESLEKQINDL 268
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNEL----------IASLEELERELEQKAEEAE--ALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865632  269 KSE-NDALNE-KLKSEEQKRRAREKANLKNPQIMylEQELESLKAVLEIKNEKLHQQDIKLMKMEK 332
Cdd:PRK00409 572 EKEaQQAIKEaKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKEKQE 635
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 105-354 6.88e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 38.80  E-value: 6.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    105 VIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARnelqtvyeaFVQQHQAEKTERENRLKEF-YTREYEK 183
Cdd:TIGR00618  630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE---------LLASRQLALQKMQSEKEQLtYWKEMLA 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    184 LRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ--ESL 261
Cdd:TIGR00618  701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgAEL 780

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    262 EKQINDLKSENDALNE-----KLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 336
Cdd:TIGR00618  781 SHLAAEIQFFNRLREEdthllKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860

                          250
                   ....*....|....*...
gi 17865632    337 NTALVDKLKRFQQENEEL 354
Cdd:TIGR00618  861 LAQLTQEQAKIIQLSDKL 878
PRK11281 PRK11281
mechanosensitive channel MscK;
229-397 8.59e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   229 KKAYEASLSEIKKG--HEIEKKSLEDLLSEKQESLEKqINDLKSENDALNEKLKSEEQKRRA--REKANLKNPQIMYLEQ 304
Cdd:PRK11281   38 EADVQAQLDALNKQklLEAEDKLVQQDLEQTLALLDK-IDRQKEETEQLKQQLAQAPAKLRQaqAELEALKDDNDEETRE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632   305 ELESLK-AVLEIKNEKL--HQQDIKlmkmEKLVDNNTALV--------------DKLKRFQQENEELKARMDKHMAISR- 366
Cdd:PRK11281  117 TLSTLSlRQLESRLAQTldQLQNAQ----NDLAEYNSQLVslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPs 192

                         170       180       190
                  ....*....|....*....|....*....|....
gi 17865632   367 ---QLSTEQAVLQESLEkeskvNKRLSMENEELL 397
Cdd:PRK11281  193 qrvLLQAEQALLNAQND-----LQRKSLEGNTQL 221
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 104-400 8.95e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.41  E-value: 8.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    104 VVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEK 183
Cdd:pfam02463  162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    184 LRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEK 263
Cdd:pfam02463  242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    264 QINDLKSENDAL----NEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKlmKMEKLVDNNTA 339
Cdd:pfam02463  322 EKKKAEKELKKEkeeiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS--AAKLKEEELEL 399

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865632    340 LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKL 400
Cdd:pfam02463  400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 163-400 9.21e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.51  E-value: 9.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    163 QAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShseklellkkayEASLSEIKKG 242
Cdd:TIGR02169  694 QSELRRIENRLDELSQE---------LSDASRKIGEIEKEIEQLEQEEEKLKERLEEL------------EEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    243 HEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLkSEEQKRRAREKANLKNPQIMYLEQELESLKAVLeikNEKLHQ 322
Cdd:TIGR02169  753 IENVKSELKELEARIEE-LEEDLHKLEEALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLREIEQKL---NRLTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632    323 QDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR-------MDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEE 395
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907


                   ....*
gi 17865632    396 LLWKL 400
Cdd:TIGR02169  908 LEAQI 912
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 79-402 9.26e-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: 38.40  E-value: 9.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632  79 ENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEkarnELQTVYEAF 158
Cdd:COG5185 160 IIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAK----EIINIEEAL 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 159 VQQhqaEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEASLSE 238
Cdd:COG5185 236 KGF---QDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFE-NTKEKIAEYTKSIDIKKAT 311

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 239 IKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNE 318
Cdd:COG5185 312 ESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKE 391

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865632 319 KLHQQDIKLMKMEKlvDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLW 398
Cdd:COG5185 392 SLDEIPQNQRGYAQ--EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAY 469


                ....
gi 17865632 399 KLHN 402
Cdd:COG5185 470 DEIN 473
 
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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