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Conserved domains on  [gi|1907070346|ref|XP_036009535|]
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trafficking kinesin-binding protein 2 isoform X10 [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 ...
 24-288 1.52e-144

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: 420.59  E-value: 1.52e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  24 RDSESITVLGTDRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHEL 103
Cdd:pfam04849  45 RETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHEL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 104 SKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQL 183
Cdd:pfam04849 125 SKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 184 VNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHE 263
Cdd:pfam04849 205 MSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQE 284

                         250       260
                  ....*....|....*....|....*
gi 1907070346 264 LQDRNMECLGMLHESQEEIKELRSK 288
Cdd:pfam04849 285 LQDRYAECLGMLHEAQEELKELRKK 309
Milton super family cl13834
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 349-500 1.24e-26

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: 106.60  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 349 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 411
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 412 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 487
Cdd:pfam12448  79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158

                         170
                  ....*....|...
gi 1907070346 488 PEKLQIVKPLEGS 500
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 ...
 24-288 1.52e-144

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: 420.59  E-value: 1.52e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  24 RDSESITVLGTDRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHEL 103
Cdd:pfam04849  45 RETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHEL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 104 SKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQL 183
Cdd:pfam04849 125 SKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 184 VNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHE 263
Cdd:pfam04849 205 MSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQE 284

                         250       260
                  ....*....|....*....|....*
gi 1907070346 264 LQDRNMECLGMLHESQEEIKELRSK 288
Cdd:pfam04849 285 LQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 349-500 1.24e-26

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: 106.60  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 349 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 411
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 412 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 487
Cdd:pfam12448  79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158

                         170
                  ....*....|...
gi 1907070346 488 PEKLQIVKPLEGS 500
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-286 1.38e-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: 54.68  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   47 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSC 126
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  127 STPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKAchiKTETFTYEEKEQQLVnDCVKELRETNAQMSRMteels 206
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA---ANLRERLESLERRIA-ATERRLEDLEEQIEEL----- 850

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  207 gksdellryQEEISSLLSQIVDLQ-------HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQ 279
Cdd:TIGR02168  851 ---------SEDIESLAAEIEELEelieeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921


                   ....*..
gi 1907070346  280 EEIKELR 286
Cdd:TIGR02168  922 EKLAQLE 928
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
6-326 1.32e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   6 NAIFkSRTGEAN--LMSSNHRDSESITVLGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNE 83
Cdd:PRK03918  128 NAIY-IRQGEIDaiLESDESREKVVRQILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIK 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  84 ALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRfnesfslsqglLQLDMLHEKLRELEEENMALR 163
Cdd:PRK03918  197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE-----------KELESLEGSKRKLEEKIRELE 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 164 SKACHIKTETFTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEhvIEKEEL 243
Cdd:PRK03918  266 ERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--LEEKEE 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 244 RLhlqaskdaqRQLTMELHELQDRNMEclgmLHESQEEIKELRSKSGPSAHLcfSQSYGVFTGESLAAEIEGTMRKKLSL 323
Cdd:PRK03918  339 RL---------EELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEI 403


                  ...
gi 1907070346 324 DEE 326
Cdd:PRK03918  404 EEE 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-287 4.10e-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: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  55 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscstplrf 132
Cdd:COG1196   212 AERYRELkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----------- 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 133 nesfslsqglLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVndcvKELRETNAQMSRMTEELSGKSDEL 212
Cdd:COG1196   281 ----------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEEL 346

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070346 213 LRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRS 287
Cdd:COG1196   347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 179-289 3.66e-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: 43.08  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  179 KEQQLVNDCVKELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 250
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907070346  251 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSKS 289
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 ...
 24-288 1.52e-144

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: 420.59  E-value: 1.52e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  24 RDSESITVLGTDRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHEL 103
Cdd:pfam04849  45 RETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHEL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 104 SKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQL 183
Cdd:pfam04849 125 SKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 184 VNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHE 263
Cdd:pfam04849 205 MSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQE 284

                         250       260
                  ....*....|....*....|....*
gi 1907070346 264 LQDRNMECLGMLHESQEEIKELRSK 288
Cdd:pfam04849 285 LQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 349-500 1.24e-26

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: 106.60  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 349 RGRSVTfPVLLPIPGSNRSSViMTAKPFESGVQP-------------AEDKTL--LSPGGSTEVPGNSQPTNP--PGSPE 411
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSS-LTSMRSSSSSTPrssyyggdgssisLDNRTNsiLSETSSSQDSGYDRPKKPgtPGTPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 412 DSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAE----QEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFM 487
Cdd:pfam12448  79 ARDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158

                         170
                  ....*....|...
gi 1907070346 488 PEKLQIVKPLEGS 500
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-286 1.38e-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: 54.68  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   47 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSC 126
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  127 STPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKAchiKTETFTYEEKEQQLVnDCVKELRETNAQMSRMteels 206
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA---ANLRERLESLERRIA-ATERRLEDLEEQIEEL----- 850

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  207 gksdellryQEEISSLLSQIVDLQ-------HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQ 279
Cdd:TIGR02168  851 ---------SEDIESLAAEIEELEelieeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921


                   ....*..
gi 1907070346  280 EEIKELR 286
Cdd:TIGR02168  922 EKLAQLE 928
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 55-333 2.27e-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: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   55 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDEllRIVSIASEesetdsscstplrf 132
Cdd:TIGR02169  210 AERYQALlkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK--RLEEIEQL-------------- 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  133 nesfslsqgllqLDMLHEKLREL-EEENMALRSKACHIKTETF----TYEEKEQQLvNDCVKELRETNAQMSRMTEELSG 207
Cdd:TIGR02169  274 ------------LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEE 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  208 KSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRS 287
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907070346  288 KsgpsahlcfsqsygvftGESLAAEIEGTMRKKLSLDEESVSKQKA 333
Cdd:TIGR02169  421 E-----------------LADLNAAIAGIEAKINELEEEKEDKALE 449
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
6-326 1.32e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   6 NAIFkSRTGEAN--LMSSNHRDSESITVLGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNE 83
Cdd:PRK03918  128 NAIY-IRQGEIDaiLESDESREKVVRQILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIK 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  84 ALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRfnesfslsqglLQLDMLHEKLRELEEENMALR 163
Cdd:PRK03918  197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE-----------KELESLEGSKRKLEEKIRELE 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 164 SKACHIKTETFTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEhvIEKEEL 243
Cdd:PRK03918  266 ERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--LEEKEE 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 244 RLhlqaskdaqRQLTMELHELQDRNMEclgmLHESQEEIKELRSKSGPSAHLcfSQSYGVFTGESLAAEIEGTMRKKLSL 323
Cdd:PRK03918  339 RL---------EELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEI 403


                  ...
gi 1907070346 324 DEE 326
Cdd:PRK03918  404 EEE 406
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 190-288 1.61e-05

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: 45.97  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 190 ELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEElrlhlqasKDAQRQLtmELHELQDRNM 269
Cdd:pfam06785  91 TLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE--------QLAEKQL--LINEYQQTIE 160

                          90
                  ....*....|....*....
gi 1907070346 270 ECLGMLHESQEEIKELRSK 288
Cdd:pfam06785 161 EQRSVLEKRQDQIENLESK 179
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 78-288 3.87e-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: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   78 LSEQNEALEEQLGQAFDQVNQLQHELSKK--DELLRIVS-IASEESETdSSCSTPLRFNESfslsqgllQLDMLHEKLRE 154
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEkIGELEAEI-ASLERSIAEKER--------ELEDAEERLAK 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  155 LEEENMALRSKACHIKTETFTYEEKEQQLVNDcVKELRETNAQMSRMTEELSGKS----DELLRYQEEISsllsqivDLQ 230
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEE-YAELKEELEDLRAELEEVDKEFaetrDELKDYREKLE-------KLK 398

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070346  231 HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 288
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-287 4.10e-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: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  55 AERDRDL--ELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscstplrf 132
Cdd:COG1196   212 AERYRELkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----------- 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 133 nesfslsqglLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVndcvKELRETNAQMSRMTEELSGKSDEL 212
Cdd:COG1196   281 ----------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEEL 346

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070346 213 LRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRS 287
Cdd:COG1196   347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
46 PHA02562
endonuclease subunit; Provisional
 151-288 4.96e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.16  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 151 KLRELEEENMALRSKACHIKTETFTYeekeqqlvNDCVKELRETNAQMsrmTEELSGKSDELLryqEEISSLLSQIVDLQ 230
Cdd:PHA02562  175 KIRELNQQIQTLDMKIDHIQQQIKTY--------NKNIEEQRKKNGEN---IARKQNKYDELV---EEAKTIKAEIEELT 240

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070346 231 HKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQ-DRNM--------ECLGMLHESQEEIKELRSK 288
Cdd:PHA02562  241 DELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkVIKMyekggvcpTCTQQISEGPDRITKIKDK 307
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-267 7.54e-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: 45.82  E-value: 7.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   35 DRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRnhvLSEQNEALEEQLgqafdqvnqlQHELSKKDELLRIVS 114
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN---LERQLEELEAQL----------EELESKLDELAEELA 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  115 IASEESETDSSCSTplRFNESFSLSQGLLQldMLHEKLRELEEENMALRSKACHIK------TETFTYEEKEQQLVNDCV 188
Cdd:TIGR02168  341 ELEEKLEELKEELE--SLEAELEELEAELE--ELESRLEELEEQLETLRSKVAQLElqiaslNNEIERLEARLERLEDRR 416

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070346  189 KELRETNAQMSRMTEELsgksdELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDR 267
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEA-----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-265 1.60e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   39 QMTKTYNDIDMVTHLLAERDRD---LELAARIGQALLKRN--------HVLSEQNEALEEQLGQAFDQVNQLQHELSKKD 107
Cdd:TIGR02168  180 KLERTRENLDRLEDILNELERQlksLERQAEKAERYKELKaelrelelALLVLRLEELREELEELQEELKEAEEELEELT 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  108 ELLRIVSIASEESEtdsscstpLRFNEsfslsqgllqldmLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVNDc 187
Cdd:TIGR02168  260 AELQELEEKLEELR--------LEVSE-------------LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ- 317

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070346  188 VKELRETNAQMSRMTEELSgksDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQ 265
Cdd:TIGR02168  318 LEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
COG5022 COG5022
Myosin heavy chain [General function prediction only];
59-453 2.08e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   59 RDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESEtdsscSTPLRFNESFSL 138
Cdd:COG5022    843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELE-----SEIIELKKSLSS 917

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  139 SQgLLQLDMLHEKLRELEEENMALRSKAchIKTETFTYEEKEQQLVNDCvKELRETNAQMSRM-------TEELSGKSDE 211
Cdd:COG5022    918 DL-IENLEFKTELIARLKKLLNNIDLEE--GPSIEYVKLPELNKLHEVE-SKLKETSEEYEDLlkkstilVREGNKANSE 993

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  212 LLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASK-----DAQRQLTMELHELQDRNMEclgMLHESQEEIKELR 286
Cdd:COG5022    994 LKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKiisseSTELSILKPLQKLKGLLLL---ENNQLQARYKALK 1070

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  287 SKSgPSAHLCFSQSYGVFTGESLAAEIEgtMRKKLSLDEESVSKQKAQQKRVFDTVKVANDTRgrsvtfpvllpIPGSNR 366
Cdd:COG5022   1071 LRR-ENSLLDDKQLYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQE-----------ISKFLS 1136

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  367 SSVIMTAKPFESgvqpaEDKTLLSPGGSTEVPGNSQPTNPP---GSPEDSDLATALH----RLSLRRQNYLSEK-----Q 434
Cdd:COG5022   1137 QLVNTLEPVFQK-----LSVLQLELDGLFWEANLEALPSPPpfaALSEKRLYQSALYdeksKLSSSEVNDLKNElialfS 1211

                          410
                   ....*....|....*....
gi 1907070346  435 FFAEEWERKIQILAEQEEE 453
Cdd:COG5022   1212 KIFSGWPRGDKLKKLISEG 1230
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 142-288 2.45e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 142 LLQLDMLHEKLRELEEEnmalrskachiktetftyEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISS 221
Cdd:COG1196   231 LLKLRELEAELEELEAE------------------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070346 222 LLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 288
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 179-289 3.66e-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: 43.08  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  179 KEQQLVNDCVKELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 250
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907070346  251 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSKS 289
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQL 280
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 146-285 5.30e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.90  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 146 DMLHEKLRELEEENMALRSKACHIKtETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKS---DELLRYQEEISSL 222
Cdd:PRK04778  313 DTLPDFLEHAKEQNKELKEEIDRVK-QSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEiaySELQEELEEILKQ 391

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 223 LSQIVDLQHKLKEHV--IEKEELRLHlQASKDAQRQLTMELHELQDRNM-----ECLGMLHESQEEIKEL 285
Cdd:PRK04778  392 LEEIEKEQEKLSEMLqgLRKDELEAR-EKLERYRNKLHEIKRYLEKSNLpglpeDYLEMFFEVSDEIEAL 460
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
 78-266 5.37e-04

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: 42.76  E-value: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  78 LSEQN-EALEEQLGQAFDQVNQLQHELSK-----KDELLRIVS-IASEESETDSSCSTPLRFNESFSLSQGLLQL----- 145
Cdd:pfam04108 109 IDEDSvEILRDALKELIDELQAAQESLDSdlkrfDDDLRDLQKeLESLSSPSESISLIPTLLKELESLEEEMASLleslt 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 146 ---DMLHEKLRELEEEnmalrskachiKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSL 222
Cdd:pfam04108 189 nhyDQCVTAVKLTEGG-----------RAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSA 257

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907070346 223 LSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQD 266
Cdd:pfam04108 258 LQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLRE 301
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
53-257 7.00e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  53 LLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSscstplrf 132
Cdd:COG4717    68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-------- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 133 nesfslsqgllQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDEL 212
Cdd:COG4717   140 -----------ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907070346 213 LRYQEEISSLLSQIVDLQHKLKEhvIEKEELRLHLQASKDAQRQL 257
Cdd:COG4717   209 AELEEELEEAQEELEELEEELEQ--LENELEAAALEERLKEARLL 251
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-337 7.37e-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: 42.74  E-value: 7.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   78 LSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETdsscstplrfnesfslsqgllQLDMLHEKLRELEE 157
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR---------------------QISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  158 EnmalrskachiktetftyEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHV 237
Cdd:TIGR02168  741 E------------------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  238 IEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSKsgpsahlcfsqsygvftGESLAAEIE--G 315
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-----------------IESLAAEIEelE 865

                          250       260
                   ....*....|....*....|..
gi 1907070346  316 TMRKKLSLDEESVSKQKAQQKR 337
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEE 887
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 147-288 9.38e-04

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: 41.61  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 147 MLHEKLRELEEENMALRSKachikteTFTYEEKeqqlVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEeISSLLSQI 226
Cdd:pfam15294 130 LLHMEIERLKEENEKLKER-------LKTLESQ----ATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKE-ISDLEEKM 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070346 227 ----VDLQHKLKEHVIEKEELRLHLQASK----DAQRQLTMELHEL--------QDRNMEclGMLHESQEEIKELRSK 288
Cdd:pfam15294 198 aalkSDLEKTLNASTALQKSLEEDLASTKhellKVQEQLEMAEKELekkfqqtaAYRNMK--EMLTKKNEQIKELRKR 273
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 54-288 9.92e-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: 42.36  E-value: 9.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   54 LAERDRDLELAARIGQ-------ALLKRNHVLSEQNEAL------EEQLGQAFDQVNQLQHELSKKDELLrivsiasEES 120
Cdd:TIGR02169  670 RSEPAELQRLRERLEGlkrelssLQSELRRIENRLDELSqelsdaSRKIGEIEKEIEQLEQEEEKLKERL-------EEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  121 ETD-SSCSTPLRFNESfSLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYE-EKEQQLVNDCVKELRETNAQM 198
Cdd:TIGR02169  743 EEDlSSLEQEIENVKS-ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  199 SRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHES 278
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901

                          250
                   ....*....|
gi 1907070346  279 QEEIKELRSK 288
Cdd:TIGR02169  902 ERKIEELEAQ 911
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 81-288 1.11e-03

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: 42.03  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   81 QNEALEEQLGQAFDQVNQLQHEL--------SKKDELLRIVSIASEESeTDSSCSTPLRFNESFSLSQGLLQLDM-LHEK 151
Cdd:pfam15921  311 QNSMYMRQLSDLESTVSQLRSELreakrmyeDKIEELEKQLVLANSEL-TEARTERDQFSQESGNLDDQLQKLLAdLHKR 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  152 LREL---EEENMAL--RSKACHIKTETFTYE----EKEQQLVNDCVKELR-ETNAQMSRMTEELSGKSDELlryqEEISS 221
Cdd:pfam15921  390 EKELsleKEQNKRLwdRDTGNSITIDHLRRElddrNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESL----EKVSS 465

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070346  222 LLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHElQDRNMEClgmlheSQEEIKELRSK 288
Cdd:pfam15921  466 LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEA------TNAEITKLRSR 525
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 150-285 1.34e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 41.57  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 150 EKLRELEEENMALRSKAcHIKTETftYEE---KEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQI 226
Cdd:pfam10168 575 QELQSLEEERKSLSERA-EKLAEK--YEEikdKQEKLMRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAI 651

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070346 227 VDLQHKlkehvieKEELRLHLQASKDAQRQLTMELHELQDRNMEclGMLHESQEEIKEL 285
Cdd:pfam10168 652 KQAKKK-------MNYQRYQIAKSQSIRKKSSLSLSEKQRKTIK--EILKQLGSEIDEL 701
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
53-244 1.49e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  53 LLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLgqafDQVNQLQHELSKKDEllRIVSIASEESETDsscstplrf 132
Cdd:COG4717    51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEE--ELEELEAELEELR--------- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 133 NESFSLSQgLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLvNDCVKELRETNAQMSRMTEELS-GKSDE 211
Cdd:COG4717   116 EELEKLEK-LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEL-EELEAELAELQEELEELLEQLSlATEEE 193

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907070346 212 LLRYQEEISSLLSQIVDLQHKLKEHVIEKEELR 244
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEEAQEELEELE 226
PLN02939 PLN02939
transferase, transferring glycosyl groups
 10-327 2.03e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.43  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  10 KSRTGEANLMSSNHRDSESITVLGTDRVEQMtKTYNDI------DMVTHLL-AERDRDLELAARIgQALLKRNHVLSEQn 82
Cdd:PLN02939   89 KSTSSDDDHNRASMQRDEAIAAIDNEQQTNS-KDGEQLsdfqleDLVGMIQnAEKNILLLNQARL-QALEDLEKILTEK- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  83 EALEEQlgqafdqVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEEENMAL 162
Cdd:PLN02939  166 EALQGK-------INILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLL 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 163 RSKACHIKTETFTYEEKEQQLVndcvkELRETNAQMSRMTEELSGKsdeLLRYQEEISSLLSQIVD--------LQHKLK 234
Cdd:PLN02939  239 KDDIQFLKAELIEVAETEERVF-----KLEKERSLLDASLRELESK---FIVAQEDVSKLSPLQYDcwwekvenLQDLLD 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 235 EHVIEKEELRLHLQASKDAQRQLTMELHELQDRNM--ECLGMLHESQEEIKELRSKSGPSAHLCFSQsygVFTGESLAAE 312
Cdd:PLN02939  311 RATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVskFSSYKVELLQQKLKLLEERLQASDHEIHSY---IQLYQESIKE 387

                         330
                  ....*....|....*
gi 1907070346 313 IEGTMRKklsLDEES 327
Cdd:PLN02939  388 FQDTLSK---LKEES 399
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
137-267 2.54e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 137 SLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQL---VNDCVKELRETNAQMSRMTEELSGKSDELL 213
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLeeeLEELNEQLQAAQAELAQAQEELESLQEEAE 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907070346 214 RYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDR 267
Cdd:COG4372   112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
51-288 6.60e-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: 6.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   51 THLLAERDrdleLAARIGQAL-----LKRNH----VLSEQNEALEeQLGQAFDQVNQLQHELSKKDELLRIVsiaseese 121
Cdd:COG4913    215 EYMLEEPD----TFEAADALVehfddLERAHealeDAREQIELLE-PIRELAERYAAARERLAELEYLRAAL-------- 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  122 tdsscstPLRFNEsfsLSQGLLQ--LDMLHEKLRELEEENMALRSKACHIKTEtftYEEKEQQLVNDCVKELRETNAQMS 199
Cdd:COG4913    282 -------RLWFAQ---RRLELLEaeLEELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGDRLEQLEREIE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  200 RMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHvieKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQ 279
Cdd:COG4913    349 RLERELEERERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425


                   ....*....
gi 1907070346  280 EEIKELRSK 288
Cdd:COG4913    426 AEIASLERR 434
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 34-265 7.24e-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: 39.67  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   34 TDRVEQMTKTYNDIDMVTHLLAERDRDL--ELAARIGQALLKrnhvLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLR 111
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKIGE----LEAEIASLERSIAEKERELEDAEERLAKLEAEID 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  112 IVSIASEESETDsscstplrfnesfsLSQGLLQLDMLHEKLRELEEENMALRSKACHIKT---ETFTYEEKEQQLVNDCV 188
Cdd:TIGR02169  333 KLLAEIEELERE--------------IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELKDYREKLEKLK 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  189 KELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQ--------------ASKDAQ 254
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEqlaadlskyeqelyDLKEEY 478

                          250
                   ....*....|.
gi 1907070346  255 RQLTMELHELQ 265
Cdd:TIGR02169  479 DRVEKELSKLQ 489
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-286 7.31e-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: 39.65  E-value: 7.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  144 QLDMLH------EKLRELEEEnmaLRSKACHIKTETFTYEEKEQQLVNdcvKELRETNAQMSRMTEELSGKSDELLRYQE 217
Cdd:TIGR02168  201 QLKSLErqaekaERYKELKAE---LRELELALLVLRLEELREELEELQ---EELKEAEEELEELTAELQELEEKLEELRL 274

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070346  218 EISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQL-------TMELHELQDRNMECLGMLHESQEEIKELR 286
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLerqleelEAQLEELESKLDELAEELAELEEKLEELK 350
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
54-290 8.22e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  54 LAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSK-KDELLRIVSIASEESETdsscstpLRF 132
Cdd:PRK03918  226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKELKEKAEEY-------IKL 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 133 NEsfslsqgllQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLvndcvKELRETNAQMSRMTEELSGKSDEL 212
Cdd:PRK03918  299 SE---------FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-----EELKKKLKELEKRLEELEERHELY 364

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070346 213 lryqEEISSLLSQIVDLQHKLKEHviEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSKSG 290
Cdd:PRK03918  365 ----EEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 54-302 8.39e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 8.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  54 LAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSScstplrfn 133
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-------- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 134 esfSLSQGLLQLDMLHEKLRELEEENMALRSkachiktETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELL 213
Cdd:COG4942   101 ---AQKEELAELLRALYRLGRQPPLALLLSP-------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 214 RYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQltmELHELQDRNMECLGMLHESQEEIKELRSKSGPSA 293
Cdd:COG4942   171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247


                  ....*....
gi 1907070346 294 hlcFSQSYG 302
Cdd:COG4942   248 ---FAALKG 253
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 54-288 8.66e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.24  E-value: 8.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  54 LAERDRDLELAARIGQALLKRnhvlseqneaLEEQLGQAFDQVNQLQHELSK-KDELLRIVSIASEESETDSSCSTPLRF 132
Cdd:pfam05667 231 LASRLTPEEYRKRKRTKLLKR----------IAEQLRSAALAGTEATSGASRsAQDLAELLSSFSGSSTTDTGLTKGSRF 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 133 NESfslsqgllqldmlhEKLRELEEENMALRSKACHIKTETFTYEEKE------QQLVNDCVKELRETNAQMSRMTEELS 206
Cdd:pfam05667 301 THT--------------EKLQFTNEAPAATSSPPTKVETEEELQQQREeeleelQEQLEDLESSIQELEKEIKKLESSIK 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 207 GKSDELLRYQEEISSLLSQIvdlqhKLKEHVIE--------KEELRLHLQASKD-----------AQRQLTMELHELQDR 267
Cdd:pfam05667 367 QVEEELEELKEQNEELEKQY-----KVKKKTLDllpdaeenIAKLQALVDASAQrlvelagqwekHRVPLIEEYRALKEA 441

                         250       260
                  ....*....|....*....|....
gi 1907070346 268 NMEclgMLHESQ---EEIKELRSK 288
Cdd:pfam05667 442 KSN---KEDESQrklEEIKELREK 462
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
170-288 9.24e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 9.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 170 KTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQA 249
Cdd:COG4372    12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907070346 250 SKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSK 288
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
46 PHA02562
endonuclease subunit; Provisional
 6-243 9.25e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.84  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346   6 NAIFKSRTGEANlmssnhRDSESITVLgTDRVEQMTKTYNDI---------DMVTHLLAERDRDLELAARIGQALLKRNH 76
Cdd:PHA02562  169 DKLNKDKIRELN------QQIQTLDMK-IDHIQQQIKTYNKNieeqrkkngENIARKQNKYDELVEEAKTIKAEIEELTD 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346  77 VLSEQNEALEEQLGqAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLR---------FNESFSLSQGLLQLDM 147
Cdd:PHA02562  242 ELLNLVMDIEDPSA-ALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQISegpdritkiKDKLKELQHSLEKLDT 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070346 148 LHEKLRELEEENMALRSKACHIKTEtftYEEKEQQLVNdCVKELRETNAQMSRMteelsgkSDELLRYQEEISSLLSQIV 227
Cdd:PHA02562  321 AIDELEEIMDEFNEQSKKLLELKNK---ISTNKQSLIT-LVDKAKKVKAAIEEL-------QAEFVDNAEELAKLQDELD 389

                         250
                  ....*....|....*.
gi 1907070346 228 DLQHKLKEHVIEKEEL 243
Cdd:PHA02562  390 KIVKTKSELVKEKYHR 405
 
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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