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Conserved domains on  [gi|12862664|dbj|BAB32550|]
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amyotrophic lateral sclerosis 2 [Homo sapiens]

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 ...
 48-353 5.54e-157

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: 462.57  E-value: 5.54e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    48 EEQLPQYRLKVDTLF-LYENQDW-TQSPH-QRQHASDALSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849   1 EEQIPPYKLRADTLGtGYANQDWkIPSPAgRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   125 DLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849  81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   205 QGLLQLEMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQLVSDCVKELRETNAQMSRMTEELSGKSDELIRYQEEL 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12862664   285 SSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSR 353
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton super family cl13834
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 415-567 6.05e-29

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: 113.92  E-value: 6.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   415 RGRSISfPALLPIPGSNRSSVIMTAKPFESGLQQT------------EDK--SLLNQGSSSEEVA-GSSQKMGQPGPSGD 479
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSSLTSMRSSSSSTPRSsyyggdgssislDNRtnSILSETSSSQDSGyDRPKKPGTPGTPGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   480 SDLATALHRLSLRRQNYLSEKQFFAEEWQRKIQVLA-----DQKEGvSGCVTPIESLASLCTTQSEITDLSSASCLRGFM 554
Cdd:pfam12448  80 RDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAgtynyDEGEH-GGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158

                         170
                  ....*....|...
gi 12862664   555 PEKLQIVKPLEGS 567
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 ...
 48-353 5.54e-157

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: 462.57  E-value: 5.54e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    48 EEQLPQYRLKVDTLF-LYENQDW-TQSPH-QRQHASDALSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849   1 EEQIPPYKLRADTLGtGYANQDWkIPSPAgRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   125 DLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849  81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   205 QGLLQLEMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQLVSDCVKELRETNAQMSRMTEELSGKSDELIRYQEEL 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12862664   285 SSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSR 353
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 415-567 6.05e-29

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: 113.92  E-value: 6.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   415 RGRSISfPALLPIPGSNRSSVIMTAKPFESGLQQT------------EDK--SLLNQGSSSEEVA-GSSQKMGQPGPSGD 479
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSSLTSMRSSSSSTPRSsyyggdgssislDNRtnSILSETSSSQDSGyDRPKKPGTPGTPGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   480 SDLATALHRLSLRRQNYLSEKQFFAEEWQRKIQVLA-----DQKEGvSGCVTPIESLASLCTTQSEITDLSSASCLRGFM 554
Cdd:pfam12448  80 RDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAgtynyDEGEH-GGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158

                         170
                  ....*....|...
gi 12862664   555 PEKLQIVKPLEGS 567
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 244-354 1.40e-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: 45.01  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    244 KEQQLVSDCVKELRETNAQMSRMTEEL--------SGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQAS 315
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 12862664    316 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSRS 354
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQL 280
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 242-391 2.32e-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: 45.06  E-value: 2.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    242 EEKEQQLvSDCVKELRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQ 321
Cdd:TIGR02169  311 AEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    322 LTMELHELQDRNMECLGMLHESQEEIKELRSRsgptahlyfsqsygaftGESLAAEIEGTMRKKLSLDEE 391
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEE-----------------LADLNAAIAGIEAKINELEEE 442
COG5022 COG5022
Myosin heavy chain [General function prediction only];
124-403 9.64e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.14  E-value: 9.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  124 RDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDELLRIVSIASEESE---TDSSCST-PLRFNE 199
Cdd:COG5022  843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELEseiIELKKSLsSDLIEN 922

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  200 SFSLSQGLLQLEMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQlvsdcvKELRETNAQMSRMTEELSGKSDELIR 279
Cdd:COG5022  923 LEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETS------EEYEDLLKKSTILVREGNKANSELKN 996

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  280 YQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASK-----DAQRQLTMELHELQDRNMEclgMLHESQEEIKELRSRS 354
Cdd:COG5022  997 FKKELAELSKQYGALQESTKQLKELPVEVAELQSASKiisseSTELSILKPLQKLKGLLLL---ENNQLQARYKALKLRR 1073

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 12862664  355 gPTAHLYFSQSYGAFTGESLAAEIEGT---MRKKLSLDEESSLFKQKAQQKR 403
Cdd:COG5022 1074 -ENSLLDDKQLYQLESTENLLKTINVKdleVTNRNLVKPANVLQFIVAQMIK 1124
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-398 4.20e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   96 ILGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDELL 175
Cdd:PRK03918 154 ILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  176 RIVSIASEESEtdsscSTPLRFNESfslsqgLLQLEMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQLvsdcvKE 255
Cdd:PRK03918 224 EKLEKEVKELE-----ELKEEIEEL------EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KE 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  256 LRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEhvIEKEELKLhlqaskdaqRQLTMELHELQDRNME 335
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--LEEKEERL---------EELKKKLKELEKRLEE 356

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12862664  336 clgmLHESQEEIKELRSRSGPTAHLyfSQSYGAFTGESLAAEIEGTMRKKLSLDEESSLFKQK 398
Cdd:PRK03918 357 ----LEERHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
 
Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 48-353 5.54e-157

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: 462.57  E-value: 5.54e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    48 EEQLPQYRLKVDTLF-LYENQDW-TQSPH-QRQHASDALSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849   1 EEQIPPYKLRADTLGtGYANQDWkIPSPAgRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   125 DLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849  81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   205 QGLLQLEMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQLVSDCVKELRETNAQMSRMTEELSGKSDELIRYQEEL 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12862664   285 SSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSR 353
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 415-567 6.05e-29

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: 113.92  E-value: 6.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   415 RGRSISfPALLPIPGSNRSSVIMTAKPFESGLQQT------------EDK--SLLNQGSSSEEVA-GSSQKMGQPGPSGD 479
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSSLTSMRSSSSSTPRSsyyggdgssislDNRtnSILSETSSSQDSGyDRPKKPGTPGTPGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   480 SDLATALHRLSLRRQNYLSEKQFFAEEWQRKIQVLA-----DQKEGvSGCVTPIESLASLCTTQSEITDLSSASCLRGFM 554
Cdd:pfam12448  80 RDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAgtynyDEGEH-GGSLTPNDSIMSLGSNHSGSSSHSSGFSSRSYL 158

                         170
                  ....*....|...
gi 12862664   555 PEKLQIVKPLEGS 567
Cdd:pfam12448 159 PEKLQIVKPLEGS 171
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 255-353 6.60e-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: 44.81  E-value: 6.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   255 ELRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEElklhlqasKDAQRQLtmELHELQDRNM 334
Cdd:pfam06785  91 TLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE--------QLAEKQL--LINEYQQTIE 160

                          90
                  ....*....|....*....
gi 12862664   335 ECLGMLHESQEEIKELRSR 353
Cdd:pfam06785 161 EQRSVLEKRQDQIENLESK 179
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 244-354 1.40e-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: 45.01  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    244 KEQQLVSDCVKELRETNAQMSRMTEEL--------SGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQAS 315
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 12862664    316 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELRSRS 354
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLKEQL 280
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 242-391 2.32e-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: 45.06  E-value: 2.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    242 EEKEQQLvSDCVKELRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQ 321
Cdd:TIGR02169  311 AEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    322 LTMELHELQDRNMECLGMLHESQEEIKELRSRsgptahlyfsqsygaftGESLAAEIEGTMRKKLSLDEE 391
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEE-----------------LADLNAAIAGIEAKINELEEE 442
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 104-403 4.96e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   104 QMTKTYNDIDMVTHLLAE-RDRDLELAARIG------QALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELckkDELLR 176
Cdd:pfam05483 248 QITEKENKMKDLTFLLEEsRDKANQLEEKTKlqdenlKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL---QIATK 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   177 IVSIASEESETDSSCSTPLRFNESFSLSQ---------GLLQLEM--LQEKLKELEEENMALRSKACHIKTET------- 238
Cdd:pfam05483 325 TICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcsleELLRTEQqrLEKNEDQLKIITMELQKKSSELEEMTkfknnke 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   239 VTYEEKEQQLVSDcvKELRETNAQMSRMTEELSGKSDELI----RYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQA 314
Cdd:pfam05483 405 VELEELKKILAED--EKLLDEKKQFEKIAEELKGKEQELIfllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   315 SKDAQRQLTMELHELQDRNMEclgMLHESQEEIKELRSRSGPTAHLYFSQsygaftgESLAAEIEGTMRKKLSLDEESSL 394
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKE---LTQEASDMTLELKKHQEDIINCKKQE-------ERMLKQIENLEEKEMNLRDELES 552


                  ....*....
gi 12862664   395 FKQKAQQKR 403
Cdd:pfam05483 553 VREEFIQKG 561
COG5022 COG5022
Myosin heavy chain [General function prediction only];
124-403 9.64e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.14  E-value: 9.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  124 RDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDELLRIVSIASEESE---TDSSCST-PLRFNE 199
Cdd:COG5022  843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELEseiIELKKSLsSDLIEN 922

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  200 SFSLSQGLLQLEMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQlvsdcvKELRETNAQMSRMTEELSGKSDELIR 279
Cdd:COG5022  923 LEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETS------EEYEDLLKKSTILVREGNKANSELKN 996

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  280 YQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASK-----DAQRQLTMELHELQDRNMEclgMLHESQEEIKELRSRS 354
Cdd:COG5022  997 FKKELAELSKQYGALQESTKQLKELPVEVAELQSASKiisseSTELSILKPLQKLKGLLLL---ENNQLQARYKALKLRR 1073

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 12862664  355 gPTAHLYFSQSYGAFTGESLAAEIEGT---MRKKLSLDEESSLFKQKAQQKR 403
Cdd:COG5022 1074 -ENSLLDDKQLYQLESTENLLKTINVKdleVTNRNLVKPANVLQFIVAQMIK 1124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
244-353 2.05e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664 244 KEQQLVSDCVKELRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQLT 323
Cdd:COG4372  21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                        90       100       110
                ....*....|....*....|....*....|
gi 12862664 324 MELHELQDRNMECLGMLHESQEEIKELRSR 353
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQ 130
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 242-351 2.11e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664 242 EEKEQQLVSDcVKELRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQ 321
Cdd:COG1196 249 EELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                        90       100       110
                ....*....|....*....|....*....|
gi 12862664 322 LTMELHELQDRNMECLGMLHESQEEIKELR 351
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAE 357
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 245-353 3.64e-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: 41.26  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    245 EQQLVSDCVKELR-ETNAQMSRMTEELSGKSDELiryqEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQLT 323
Cdd:pfam15921  427 EVQRLEALLKAMKsECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLT 502

                           90       100       110
                   ....*....|....*....|....*....|
gi 12862664    324 MELHElQDRNMEClgmlheSQEEIKELRSR 353
Cdd:pfam15921  503 ASLQE-KERAIEA------TNAEITKLRSR 525
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-398 4.20e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664   96 ILGTDRVEqmtKTYNDIDMVTHLLAERDRDLElaarigqALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDELL 175
Cdd:PRK03918 154 ILGLDDYE---NAYKNLGEVIKEIKRRIERLE-------KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  176 RIVSIASEESEtdsscSTPLRFNESfslsqgLLQLEMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQLvsdcvKE 255
Cdd:PRK03918 224 EKLEKEVKELE-----ELKEEIEEL------EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KE 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664  256 LRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEhvIEKEELKLhlqaskdaqRQLTMELHELQDRNME 335
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--LEEKEERL---------EELKKKLKELEKRLEE 356

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12862664  336 clgmLHESQEEIKELRSRSGPTAHLyfSQSYGAFTGESLAAEIEGTMRKKLSLDEESSLFKQK 398
Cdd:PRK03918 357 ----LEERHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 254-404 5.47e-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: 40.13  E-value: 5.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664 254 KELRETNAQMSRMTEELSGKSDELIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQLTMELHELQDRN 333
Cdd:COG4942  27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12862664 334 MECLGML--HESQEEIKELRSRSGPTAHLYFSQSYGAFTgESLAAEIEGTMRKKLSLDEESSLFKQKAQQKRV 404
Cdd:COG4942 107 AELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAERAELEA 178
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-353 7.14e-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: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    112 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELCKKDEllRIVSIASEESETDSSC 191
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA--EIEELEERLEEAEEEL 777

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    192 STPLRfnESFSLSQGLLQL-EMLQEKLKELEEENMALRSKACHIKTETVTYEEKEQQlVSDCVKELRETNAQMSRMTEEL 270
Cdd:TIGR02168  778 AEAEA--EIEELEAQIEQLkEELKALREALDELRAELTLLNEEAANLRERLESLERR-IAATERRLEDLEEQIEELSEDI 854

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    271 sgksdelIRYQEELSSLLSQIVDLQHKLKEHVIEKEELKLHLQASKDAQRQLtmelhelqdrnmeclgmlhesQEEIKEL 350
Cdd:TIGR02168  855 -------ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL---------------------SEELREL 906


                   ...
gi 12862664    351 RSR 353
Cdd:TIGR02168  907 ESK 909
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 119-346 9.85e-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: 9.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    119 LAERDRDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELC----KKDELLRIVSIASEESETDSSCSTP 194
Cdd:TIGR02168  728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeaeaEIEELEAQIEQLKEELKALREALDE 807

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    195 LRfNESFSLSQGLLQLEmlqeklkeLEEENMALRSKACHIKTETVTYE-EKEQQLVSDCVKELRETNAQMSRMTEELSGK 273
Cdd:TIGR02168  808 LR-AELTLLNEEAANLR--------ERLESLERRIAATERRLEDLEEQiEELSEDIESLAAEIEELEELIEELESELEAL 878

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12862664    274 SDELIRYQEELSSLLSQIVDLQHKLKEHVIEK-------EELKLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEE 346
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSEELRELESKRselrrelEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
 
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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