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Conserved domains on  [gi|1907070330|ref|XP_036009520|]
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trafficking kinesin-binding protein 2 isoform X2 [Mus musculus]

Protein Classification

HAP1_N and Milton domain-containing protein( domain architecture ID 12058642)

HAP1_N and Milton domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 48-372 4.20e-164

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


:

Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 481.45  E-value: 4.20e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  48 EEQLPQYKLRVDSLF-LYENQDWA--QSSHQQQDAPETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849   1 EEQIPPYKLRADTLGtGYANQDWKipSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 125 DLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849  81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 205 QGLLQLDMLHEKLRELEEENMALRSkvqfaslssnalwaalgdaEACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSR 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRS-------------------EASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAE 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 285 MTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQE 364
Cdd:pfam04849 222 LSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQE 301


                  ....*...
gi 1907070330 365 EIKELRSK 372
Cdd:pfam04849 302 ELKELRKK 309
Milton super family cl13834
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 433-584 1.31e-25

Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.


The actual alignment was detected with superfamily member pfam12448:

Pssm-ID: 463588  Cd Length: 171  Bit Score: 104.29  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 433 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 495
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 496 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 571
Cdd:pfam12448  79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158

                         170
                  ....*....|...
gi 1907070330 572 PEKLQIVKPLEGS 584
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
 
Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 48-372 4.20e-164

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 481.45  E-value: 4.20e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  48 EEQLPQYKLRVDSLF-LYENQDWA--QSSHQQQDAPETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849   1 EEQIPPYKLRADTLGtGYANQDWKipSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 125 DLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849  81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 205 QGLLQLDMLHEKLRELEEENMALRSkvqfaslssnalwaalgdaEACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSR 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRS-------------------EASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAE 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 285 MTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQE 364
Cdd:pfam04849 222 LSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQE 301


                  ....*...
gi 1907070330 365 EIKELRSK 372
Cdd:pfam04849 302 ELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 433-584 1.31e-25

Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.


Pssm-ID: 463588  Cd Length: 171  Bit Score: 104.29  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 433 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 495
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 496 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 571
Cdd:pfam12448  79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158

                         170
                  ....*....|...
gi 1907070330 572 PEKLQIVKPLEGS 584
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-369 3.13e-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: 57.76  E-value: 3.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  112 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSC 191
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  192 STPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAcHIKTETFTYEEKEQQLVNdC 271
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER-RLEDLEEQIEELSEDIES-L 857

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  272 VKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDR 351
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                          250       260
                   ....*....|....*....|..
gi 1907070330  352 NMECLGMLHE----SQEEIKEL 369
Cdd:TIGR02168  938 IDNLQERLSEeyslTLEEAEAL 959
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-371 7.20e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 120 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscstplrf 197
Cdd:COG1196   212 AERYRELkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----------- 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 198 nesfslsqglLQLDMLHEKLRELEEENMALRSKVQFASLSSNALwaalgdaeachiktetftyEEKEQQLVndcvKELRE 277
Cdd:COG1196   281 ----------LELEEAQAEEYELLAELARLEQDIARLEERRREL-------------------EERLEELE----EELAE 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 278 TNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLG 357
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         250
                  ....*....|....
gi 1907070330 358 MLHESQEEIKELRS 371
Cdd:COG1196   408 AEEALLERLERLEE 421
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-410 1.37e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  96 ILGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELL 175
Cdd:PRK03918  154 ILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 176 RIVSIASEESEtdsscSTPLRFNESFSLSQGLLQ-LDMLHEKLRELEEENMALRSKVQfaslssnalwaalgdaeachik 254
Cdd:PRK03918  224 EKLEKEVKELE-----ELKEEIEELEKELESLEGsKRKLEEKIRELEERIEELKKEIE---------------------- 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 255 tetfTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEhvIEKEELRLhlqas 334
Cdd:PRK03918  277 ----ELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--LEEKEERL----- 340

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070330 335 kdaqRQLTMELHELQDRNMEclgmLHESQEEIKELRSKSGPSAHLcfSQSYGVFTGESLAAEIEGTMRKKLSLDEE 410
Cdd:PRK03918  341 ----EELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEIEEE 406
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 263-373 1.68e-04

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: 44.62  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  263 KEQQLVNDCVKELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 334
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907070330  335 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSKS 373
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQL 280
 
Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 48-372 4.20e-164

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 481.45  E-value: 4.20e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  48 EEQLPQYKLRVDSLF-LYENQDWA--QSSHQQQDAPETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849   1 EEQIPPYKLRADTLGtGYANQDWKipSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 125 DLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849  81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 205 QGLLQLDMLHEKLRELEEENMALRSkvqfaslssnalwaalgdaEACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSR 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRS-------------------EASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAE 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 285 MTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQE 364
Cdd:pfam04849 222 LSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQE 301


                  ....*...
gi 1907070330 365 EIKELRSK 372
Cdd:pfam04849 302 ELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 433-584 1.31e-25

Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.


Pssm-ID: 463588  Cd Length: 171  Bit Score: 104.29  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 433 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 495
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 496 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 571
Cdd:pfam12448  79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158

                         170
                  ....*....|...
gi 1907070330 572 PEKLQIVKPLEGS 584
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-369 3.13e-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: 57.76  E-value: 3.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  112 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSC 191
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  192 STPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAcHIKTETFTYEEKEQQLVNdC 271
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER-RLEDLEEQIEELSEDIES-L 857

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  272 VKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDR 351
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                          250       260
                   ....*....|....*....|..
gi 1907070330  352 NMECLGMLHE----SQEEIKEL 369
Cdd:TIGR02168  938 IDNLQERLSEeyslTLEEAEAL 959
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 143-370 2.17e-07

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: 2.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  143 LSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEE 222
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  223 ENMALRSKVQFASLSSNAL---WAAL-----GDAEACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSD 294
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAeaeIEELeaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  295 ELL----RYQEEISSLLSQIVDLQ-------HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQ 363
Cdd:TIGR02168  842 DLEeqieELSEDIESLAAEIEELEelieeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921


                   ....*..
gi 1907070330  364 EEIKELR 370
Cdd:TIGR02168  922 EKLAQLE 928
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 120-417 2.12e-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: 51.99  E-value: 2.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  120 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDEllRIVSIASEesetdsscstplrf 197
Cdd:TIGR02169  210 AERYQALlkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK--RLEEIEQL-------------- 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  198 nesfslsqgllqLDMLHEKLRELEEENMaLRSKVQFASLSSNAlwAALGDAEAchiktetftyeEKEQQLvNDCVKELRE 277
Cdd:TIGR02169  274 ------------LEELNKKIKDLGEEEQ-LRVKEKIGELEAEI--ASLERSIA-----------EKEREL-EDAEERLAK 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  278 TNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLG 357
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  358 MLHESQEEIKELRSKsgpsahlcfsqsygvftGESLAAEIEGTMRKKLSLDEESVSKQKA 417
Cdd:TIGR02169  407 ELDRLQEELQRLSEE-----------------LADLNAAIAGIEAKINELEEEKEDKALE 449
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 274-372 3.09e-06

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 48.66  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 274 ELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEElrlhlqasKDAQRQLtmELHELQDRNM 353
Cdd:pfam06785  91 TLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE--------QLAEKQL--LINEYQQTIE 160

                          90
                  ....*....|....*....
gi 1907070330 354 ECLGMLHESQEEIKELRSK 372
Cdd:pfam06785 161 EQRSVLEKRQDQIENLESK 179
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 143-372 4.63e-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: 50.84  E-value: 4.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  143 LSEQNEALEEQLGQAFDQVNQLQHELskkDELLRIVSIASEESETDSSCSTPL-----RFNESfsLSQGLLQLDMLHEKL 217
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRL---DELSQELSDASRKIGEIEKEIEQLeqeeeKLKER--LEELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  218 RELEEENMALRSKVQFASLSSNALWAALGDAEAcHIKTETFTYEEKEQQLVNDCVKE----LRETNAQMSRMTEELSGKS 293
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLEA-RLSHSRIPEIQAELSKLEEEVSRiearLREIEQKLNRLTLEKEYLE 832

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070330  294 DELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 209-421 8.54e-06

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: 49.67  E-value: 8.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  209 QLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAchiktetftYEEKEQQLVNDCVKELRETNAQMSRMTEE 288
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA---------EVEQLEERIAQLSKELTELEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  289 LSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKE 368
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907070330  369 LRSKsgpsahlcfsqsygvftGESLAAEIE--GTMRKKLSLDEESVSKQKAQQKR 421
Cdd:TIGR02168  850 LSED-----------------IESLAAEIEelEELIEELESELEALLNERASLEE 887
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-466 1.17e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  100 DRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRnhvLSEQNEALEEQLgqafdqvnqlQHELSKKDELLRIVS 179
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN---LERQLEELEAQL----------EELESKLDELAEELA 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  180 IASEESETDSSCSTplRFNESFSLSQGLLQldMLHEKLRELEEENMALRSKVQFASLSSNALwaalgdaeachikTETFT 259
Cdd:TIGR02168  341 ELEEKLEELKEELE--SLEAELEELEAELE--ELESRLEELEEQLETLRSKVAQLELQIASL-------------NNEIE 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  260 YEEKEQQLVNDCVKELRETNAQMSRMTEELsgksdELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQR 339
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEA-----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  340 QLTMELHELQDRNMECLGML--HES-QEEIKEL-RSKSGPSAHL-CFSQSYGVFTGESLAAEI--EGTMRKKLSLDEESV 412
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQenLEGfSEGVKALlKNQSGLSGILgVLSELISVDEGYEAAIEAalGGRLQAVVVENLNAA 558

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070330  413 S------KQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPG--SNRSSVIMTAKPFESGVQP 466
Cdd:TIGR02168  559 KkaiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflGVAKDLVKFDPKLRKALSY 620
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
 143-350 1.83e-05

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 48.15  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 143 LSEQN-EALEEQLGQAFDQVNQLQHELSKkdELLRIVSIASEESETDSSCSTPLRFNESFSlsqgllqlDMLHEkLRELE 221
Cdd:pfam04108 109 IDEDSvEILRDALKELIDELQAAQESLDS--DLKRFDDDLRDLQKELESLSSPSESISLIP--------TLLKE-LESLE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 222 EEnMA--LRSKVQFASLSSNALWAALGDaeachiKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRY 299
Cdd:pfam04108 178 EE-MAslLESLTNHYDQCVTAVKLTEGG------RAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSL 250

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907070330 300 QEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQD 350
Cdd:pfam04108 251 IDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLRE 301
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 153-372 2.27e-05

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 47.01  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 153 QLGQAFDQVNQ----LQHELSKKD--ELLRIVSIAsEESETDSSCSTPlrfneSFSLSQGLLQ-------LDMLHEKLRE 219
Cdd:pfam15294  64 LLRQLFSQAEKwhlkLQADISELEnrELLEQIAEF-EEREFTSSNKKP-----NFELNKPKLEplnegggSALLHMEIER 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 220 LEEENMALRSkvQFASLSSNALwAALGDAEACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDEllrY 299
Cdd:pfam15294 138 LKEENEKLKE--RLKTLESQAT-QALDEKSKLEKALKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA---S 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 300 QEEISSLLSQIVDLQHKLkehviekeeLRLhlqaskdaQRQLTMELHELQD--------RNMEclGMLHESQEEIKELRS 371
Cdd:pfam15294 212 TALQKSLEEDLASTKHEL---------LKV--------QEQLEMAEKELEKkfqqtaayRNMK--EMLTKKNEQIKELRK 272


                  .
gi 1907070330 372 K 372
Cdd:pfam15294 273 R 273
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 86-309 4.20e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330   86 VLAEETFRYMILGTDRV----EQMTKTYNDIDMVTHLLAERDRDLE-LAARIGQALLKRNHVLSEQnEALEEQLGQAFDQ 160
Cdd:TIGR02169  273 LLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEIDKLLAEI-EELEREIEEERKR 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  161 VNQLQHEL-SKKDELLRIVSIASEESEtdsscstplRFNESF-SLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSS 238
Cdd:TIGR02169  352 RDKLTEEYaELKEELEDLRAELEEVDK---------EFAETRdELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070330  239 NALWAALGDAEACHIKTETFT------YEEKEQQLvNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQ 309
Cdd:TIGR02169  423 ADLNAAIAGIEAKINELEEEKedkaleIKKQEWKL-EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-371 7.20e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 120 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscstplrf 197
Cdd:COG1196   212 AERYRELkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----------- 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 198 nesfslsqglLQLDMLHEKLRELEEENMALRSKVQFASLSSNALwaalgdaeachiktetftyEEKEQQLVndcvKELRE 277
Cdd:COG1196   281 ----------LELEEAQAEEYELLAELARLEQDIARLEERRREL-------------------EERLEELE----EELAE 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 278 TNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLG 357
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         250
                  ....*....|....
gi 1907070330 358 MLHESQEEIKELRS 371
Cdd:COG1196   408 AEEALLERLERLEE 421
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-410 1.37e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  96 ILGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELL 175
Cdd:PRK03918  154 ILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 176 RIVSIASEESEtdsscSTPLRFNESFSLSQGLLQ-LDMLHEKLRELEEENMALRSKVQfaslssnalwaalgdaeachik 254
Cdd:PRK03918  224 EKLEKEVKELE-----ELKEEIEELEKELESLEGsKRKLEEKIRELEERIEELKKEIE---------------------- 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 255 tetfTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEhvIEKEELRLhlqas 334
Cdd:PRK03918  277 ----ELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--LEEKEERL----- 340

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070330 335 kdaqRQLTMELHELQDRNMEclgmLHESQEEIKELRSKSGPSAHLcfSQSYGVFTGESLAAEIEGTMRKKLSLDEE 410
Cdd:PRK03918  341 ----EELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEIEEE 406
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 263-373 1.68e-04

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: 44.62  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  263 KEQQLVNDCVKELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 334
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907070330  335 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSKS 373
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQL 280
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 113-372 1.80e-04

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: 45.49  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  113 DMVTHLLAERDRDLE-LAARIGQALLKRNHVLSE----------QNEALEEQLGQAFDQVNQLQHEL--------SKKDE 173
Cdd:pfam15921  267 DRIEQLISEHEVEITgLTEKASSARSQANSIQSQleiiqeqarnQNSMYMRQLSDLESTVSQLRSELreakrmyeDKIEE 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  174 LLRIVSIASEESeTDSSCSTPLRFNESFSLSQGLLQLDM-LHEKLREL---EEENMALRSKVQFASLSSNALWAALGDae 249
Cdd:pfam15921  347 LEKQLVLANSEL-TEARTERDQFSQESGNLDDQLQKLLAdLHKREKELsleKEQNKRLWDRDTGNSITIDHLRRELDD-- 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  250 achiktetftyEEKEQQLVNDCVKELR-ETNAQMSRMTEELSGKSDELlryqEEISSLLSQIVDLQHKLKEHVIEKEELR 328
Cdd:pfam15921  424 -----------RNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKK 488

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907070330  329 LHLQASKDAQRQLTMELHElQDRNMEClgmlheSQEEIKELRSK 372
Cdd:pfam15921  489 MTLESSERTVSDLTASLQE-KERAIEA------TNAEITKLRSR 525
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 99-349 6.61e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 6.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330   99 TDRVEQMTKTYNDIDMVTHLLAERDRDL--ELAARIGQALLKrnhvLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLR 176
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKIGE----LEAEIASLERSIAEKERELEDAEERLAKLEAEID 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  177 IVSIASEESETDsscstplrfnesfsLSQGLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAchiKTE 256
Cdd:TIGR02169  333 KLLAEIEELERE--------------IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLE 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  257 TFTYEEKEQQLVND-CVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASK 335
Cdd:TIGR02169  396 KLKREINELKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475

                          250
                   ....*....|....
gi 1907070330  336 DAQRQLTMELHELQ 349
Cdd:TIGR02169  476 EEYDRVEKELSKLQ 489
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
254-372 7.89e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 254 KTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQA 333
Cdd:COG4372    12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907070330 334 SKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
46 PHA02562
endonuclease subunit; Provisional
 247-372 1.32e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 247 DAEACHIKTETFTYeekeqqlvNDCVKELRETNAQMsrmTEELSGKSDELLryqEEISSLLSQIVDLQHKLKEHVIEKEE 326
Cdd:PHA02562  187 DMKIDHIQQQIKTY--------NKNIEEQRKKNGEN---IARKQNKYDELV---EEAKTIKAEIEELTDELLNLVMDIED 252

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907070330 327 LRLHLQASKDAQRQLTMELHELQ-DRNM--------ECLGMLHESQEEIKELRSK 372
Cdd:PHA02562  253 PSAALNKLNTAAAKIKSKIEQFQkVIKMyekggvcpTCTQQISEGPDRITKIKDK 307
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 262-372 1.36e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 262 EKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQL 341
Cdd:COG1196   249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907070330 342 TMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:COG1196   329 EEELEELEEELEELEEELEEAEEELEEAEAE 359
COG5022 COG5022
Myosin heavy chain [General function prediction only];
124-537 1.53e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.37  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  124 RDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscSTPLRFNESFSL 203
Cdd:COG5022    843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELE-----SEIIELKKSLSS 917

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  204 SQgLLQLDMLHEKLRELEEENMALRSKVQfaslssnalwaalgdaeachiKTETFTYEEKEQQLVNDCvKELRETNAQMS 283
Cdd:COG5022    918 DL-IENLEFKTELIARLKKLLNNIDLEEG---------------------PSIEYVKLPELNKLHEVE-SKLKETSEEYE 974

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  284 RM-------TEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASK-----DAQRQLTMELHELQDR 351
Cdd:COG5022    975 DLlkkstilVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKiisseSTELSILKPLQKLKGL 1054

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  352 NMEclgMLHESQEEIKELRSKSgPSAHLCFSQSYGVFTGESLAAEIEgtMRKKLSLDEESVSKQKAQQKRVFDTVKVAND 431
Cdd:COG5022   1055 LLL---ENNQLQARYKALKLRR-ENSLLDDKQLYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLL 1128

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  432 TRgrsvtfpvllpIPGSNRSSVIMTAKPFESgvqpaEDKTLLSPGGSTEVPGNSQPTNPP---GSPEDSDLATALH---- 504
Cdd:COG5022   1129 QE-----------ISKFLSQLVNTLEPVFQK-----LSVLQLELDGLFWEANLEALPSPPpfaALSEKRLYQSALYdeks 1192

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1907070330  505 RLSLRRQNYLSEK-----QFFAEEWERKIQILAEQEEE 537
Cdd:COG5022   1193 KLSSSEVNDLKNElialfSKIFSGWPRGDKLKKLISEG 1230
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-372 2.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  47 LEEQLPQYKLRVDSLfLYENQDWAQSSHQQQDAPETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDRDL 126
Cdd:COG4717   137 LEAELAELPERLEEL-EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 127 ElaarigqallkrnhVLSEQNEALEEQLGQAFDQ--VNQLQHELSKKDELLRIVS-IASEESETDSSCSTPLRFNESFSL 203
Cdd:COG4717   216 E--------------EAQEELEELEEELEQLENEleAAALEERLKEARLLLLIAAaLLALLGLGGSLLSLILTIAGVLFL 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 204 SQGLLQLDMLH------------------EKLRELEEEN-MALRSKVQFASLSSNALWAALGDAEAcHIKTETFTYEEKE 264
Cdd:COG4717   282 VLGLLALLFLLlarekaslgkeaeelqalPALEELEEEElEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELE 360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 265 QQLvndcvkELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQrQLTME 344
Cdd:COG4717   361 EEL------QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-ELEEE 433

                         330       340
                  ....*....|....*....|....*...
gi 1907070330 345 LHELQDRnmeclgmLHESQEEIKELRSK 372
Cdd:COG4717   434 LEELEEE-------LEELEEELEELREE 454
PLN02939 PLN02939
transferase, transferring glycosyl groups
 130-411 3.19e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.43  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 130 ARIgQALLKRNHVLSEQnEALEEQlgqafdqVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQ 209
Cdd:PLN02939  150 ARL-QALEDLEKILTEK-EALQGK-------INILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLC 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 210 LDMLHEKLRELEEENMALRSKVQFASlssnalwaalgdAEACHIK-TETFTYE-EKEQQLVNDCVKELRetnAQMSRMTE 287
Cdd:PLN02939  221 VHSLSKELDVLKEENMLLKDDIQFLK------------AELIEVAeTEERVFKlEKERSLLDASLRELE---SKFIVAQE 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 288 ELSgKSDELlryqeEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNM--ECLGMLHESQEE 365
Cdd:PLN02939  286 DVS-KLSPL-----QYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVskFSSYKVELLQQK 359

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907070330 366 IKELRSKSGPSAHLCFSQsygVFTGESLAAEIEGTMRKklsLDEES 411
Cdd:PLN02939  360 LKLLEERLQASDHEIHSY---IQLYQESIKEFQDTLSK---LKEES 399
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
209-351 3.25e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 209 QLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAeachiKTETFTYEEKEQQLVndcvKELRETNAQMSRMTEE 288
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-----RSELEQLEEELEELN----EQLQAAQAELAQAQEE 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070330 289 LSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDR 351
Cdd:COG4372   103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 176-369 3.89e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  176 RIVSIASEESETDSSC---STPLRFNESFSLSQgLLQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAch 252
Cdd:TIGR02169  640 RMVTLEGELFEKSGAMtggSRAPRGGILFSRSE-PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-- 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  253 iKTETFtyeEKEQQLVNDcvkELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQ 332
Cdd:TIGR02169  717 -KIGEI---EKEIEQLEQ---EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907070330  333 ASKdaQRQLTMELHELQDRNMECLGMLHESQEEIKEL 369
Cdd:TIGR02169  790 HSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 119-386 4.01e-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: 40.52  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 119 LAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDEllRIVSIASEESEtdsscstplrfn 198
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA--ELAELEKEIAE------------ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 199 esfslsqgllqldmLHEKLRELEEEnmaLRSKVQFASLSSNALWAALGdaeachIKTETFTYEEKEQQLVNDCVKELRET 278
Cdd:COG4942    95 --------------LRAELEAQKEE---LAELLRALYRLGRQPPLALL------LSPEDFLDAVRRLQYLKYLAPARREQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 279 NAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQltmELHELQDRNMECLGM 358
Cdd:COG4942   152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEAL 228

                         250       260
                  ....*....|....*....|....*...
gi 1907070330 359 LHESQEEIKELRSKSGPSAhlcFSQSYG 386
Cdd:COG4942   229 IARLEAEAAAAAERTPAAG---FAALKG 253
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
229-372 4.33e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 229 SKVQFASLSSNALWAALGDAEAC---HIKTETFTYEEKEQQLvNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISS 305
Cdd:COG4372     6 EKVGKARLSLFGLRPKTGILIAAlseQLRKALFELDKLQEEL-EQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070330 306 LLSQIVDLQHKLKEHV-------IEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:COG4372    85 LNEQLQAAQAELAQAQeeleslqEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-349 6.47e-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: 40.43  E-value: 6.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  104 QMTKTYNDIDMVTHLLAERDRDLELAARigQA-LLKRNHVLSEQNEALEEQLgqafdQVNQLQHELSKKDELLRIVSIAS 182
Cdd:TIGR02168  180 KLERTRENLDRLEDILNELERQLKSLER--QAeKAERYKELKAELRELELAL-----LVLRLEELREELEELQEELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  183 EESETDSScstplrfnesfslsqgllQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAcHIKTetftYEE 262
Cdd:TIGR02168  253 EELEELTA------------------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ-QKQI----LRE 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  263 KEQQLVNDcVKELRETNAQMSRMTEELSgksDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLT 342
Cdd:TIGR02168  310 RLANLERQ-LEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385


                   ....*..
gi 1907070330  343 MELHELQ 349
Cdd:TIGR02168  386 SKVAQLE 392
PRK01156 PRK01156
chromosome segregation protein; Provisional
 100-372 6.56e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 100 DRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVS 179
Cdd:PRK01156  173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 180 iaseesetdsscstplRFNESFSLSQGLLQLD-MLHEKLRELEEENMALRSKVQFASLSS-NALWAALGDAEAC-----H 252
Cdd:PRK01156  253 ----------------RYESEIKTAESDLSMElEKNNYYKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKkqilsN 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 253 IKTETFTYEEKEQQLVNdcVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQ 332
Cdd:PRK01156  317 IDAEINKYHAIIKKLSV--LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS 394

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907070330 333 ASKDAQR----QLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:PRK01156  395 EILKIQEidpdAIKKELNEINVKLQDISSKVSSLNQRIRALREN 438
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
139-372 7.68e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 7.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  139 RNHVLsEQNEALE--EQLGQAFDQVNQLQHELSK----KDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDM 212
Cdd:COG4913    214 REYML-EEPDTFEaaDALVEHFDDLERAHEALEDareqIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  213 LHEKLRELEEENMALRSKVQFASlssnalwAALGDAEAchiktetfTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGK 292
Cdd:COG4913    293 LEAELEELRAELARLEAELERLE-------ARLDALRE--------ELDELEAQIRGNGGDRLEQLEREIERLERELEER 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330  293 SDELLRYQEEISSLLSQIVDLQHKLKEHvieKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 372
Cdd:COG4913    358 ERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 248-369 7.75e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 248 AEACHIKtETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKS---DELLRYQEEISSLLSQIVDLQHKLKEHV--I 322
Cdd:PRK04778  331 EEIDRVK-QSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEiaySELQEELEEILKQLEEIEKEQEKLSEMLqgL 409

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907070330 323 EKEELRLHlQASKDAQRQLTMELHELQDRNM-----ECLGMLHESQEEIKEL 369
Cdd:PRK04778  410 RKDELEAR-EKLERYRNKLHEIKRYLEKSNLpglpeDYLEMFFEVSDEIEAL 460
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 208-372 8.58e-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: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 208 LQLDMLHEKLRELEEENMALRSKVQFASLSSNALWAALGDAEAchiktetfTYEEKEQqlvndcvkELRETNAQMSRMTE 287
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK--------EIKRLEL--------EIEEVEARIKKYEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070330 288 ELSG--KSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGmlhESQEE 365
Cdd:COG1579    81 QLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAE 157


                  ....*..
gi 1907070330 366 IKELRSK 372
Cdd:COG1579   158 LEELEAE 164
 
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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