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Conserved domains on  [gi|75905813|ref|NP_598244|]
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trafficking kinesin-binding protein 2 [Rattus norvegicus]

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 8.58e-156

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: 459.49  E-value: 8.58e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    48 EEQLPQYKLRVDSLF-LYENQDWS--QSSHQQQDASETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849   1 EEQIPPYKLRADTLGtGYANQDWKipSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   125 DLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELSKKEELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849  81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   205 QGLLQLDMMHEKLKELEEENMALRSKACHIKTETFTYEEKEQKLINDCVNELRETNAQMSRMTEELSGKSDELLRYQEEI 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75905813   285 SSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRNK 353
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton super family cl13834
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
414-565 5.20e-25

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


The actual alignment was detected with superfamily member pfam12448:

Pssm-ID: 463588  Cd Length: 171  Bit Score: 102.36  E-value: 5.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   414 RGRSVTfPVLLPIPGSNRSSVIMTAKPFESGVQQT------------EDKTLPN--QGSSTEVPGNSHPRDP--PGLPED 477
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSSLTSMRSSSSSTPRSsyyggdgssislDNRTNSIlsETSSSQDSGYDRPKKPgtPGTPGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   478 SDLATALHRLSLRRQNYLSEKQFFAEEWERKLQILAEQE--EEVSSCEALT--ENLASFCTDQSETTELGSAGCLRGFMP 553
Cdd:pfam12448  80 RDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGTYnyDEGEHGGSLTpnDSIMSLGSNHSGSSSHSSGFSSRSYLP 159
                         170
                  ....*....|..
gi 75905813   554 EKLQIVKPLEGS 565
Cdd:pfam12448 160 EKLQIVKPLEGS 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 8.58e-156

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: 459.49  E-value: 8.58e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    48 EEQLPQYKLRVDSLF-LYENQDWS--QSSHQQQDASETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849   1 EEQIPPYKLRADTLGtGYANQDWKipSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   125 DLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELSKKEELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849  81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   205 QGLLQLDMMHEKLKELEEENMALRSKACHIKTETFTYEEKEQKLINDCVNELRETNAQMSRMTEELSGKSDELLRYQEEI 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75905813   285 SSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRNK 353
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
414-565 5.20e-25

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


Pssm-ID: 463588  Cd Length: 171  Bit Score: 102.36  E-value: 5.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   414 RGRSVTfPVLLPIPGSNRSSVIMTAKPFESGVQQT------------EDKTLPN--QGSSTEVPGNSHPRDP--PGLPED 477
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSSLTSMRSSSSSTPRSsyyggdgssislDNRTNSIlsETSSSQDSGYDRPKKPgtPGTPGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   478 SDLATALHRLSLRRQNYLSEKQFFAEEWERKLQILAEQE--EEVSSCEALT--ENLASFCTDQSETTELGSAGCLRGFMP 553
Cdd:pfam12448  80 RDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGTYnyDEGEHGGSLTpnDSIMSLGSNHSGSSSHSSGFSSRSYLP 159
                         170
                  ....*....|..
gi 75905813   554 EKLQIVKPLEGS 565
Cdd:pfam12448 160 EKLQIVKPLEGS 171
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
244-351 7.63e-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: 42.70  E-value: 7.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    244 KEQKLINDCVNELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 315
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 75905813    316 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELR 351
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLK 277
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
102-428 1.07e-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: 43.12  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    102 VEQMTKTYNDIDMVTHLLAE-RDRDLELAARIgQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELSKKEELLRIVSI 180
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEElRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    181 ASEESETDSSCSTplrfNESFSLSQGLLQLDMMHEKLKELEEeNMALRSKACHIKTETFtyeekeQKLINDCVNELRETN 260
Cdd:TIGR02168  331 KLDELAEELAELE----EKLEELKEELESLEAELEELEAELE-ELESRLEELEEQLETL------RSKVAQLELQIASLN 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    261 AQMSRMTEELSGKSDELLRYQEEISSLLSQ-------------------IVDLQHKLKEHVIEKEELRLHLQASKDAQRQ 321
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKleeaelkelqaeleeleeeLEELQEELERLEEALEELREELEEAEQALDA 479
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    322 LTMELHELQDRNMECLGML--HES-QEEIKEL-RNKAGPSAHL-CFSQAYGVFAGESLAAEI--EGTMRKKLSLDEESVF 394
Cdd:TIGR02168  480 AERELAQLQARLDSLERLQenLEGfSEGVKALlKNQSGLSGILgVLSELISVDEGYEAAIEAalGGRLQAVVVENLNAAK 559
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 75905813    395 ------KQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPG 428
Cdd:TIGR02168  560 kaiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
46 PHA02562
endonuclease subunit; Provisional
233-354 1.86e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813  233 HIKTETFTYeekeqkliNDCVNELRETNAQMsrmTEELSGKSDELLryqEEISSLLSQIVDLQHKLKEHVIEKEELRLHL 312
Cdd:PHA02562 192 HIQQQIKTY--------NKNIEEQRKKNGEN---IARKQNKYDELV---EEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 75905813  313 QASKDAQRQLTMELHELQ-DRNM--------ECLGMLHESQEEIKELRNKA 354
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQkVIKMyekggvcpTCTQQISEGPDRITKIKDKL 308
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
235-354 2.17e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813 235 KTETFTYEEKEQKLINDCVNELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQA 314
Cdd:COG4372  12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 75905813 315 SKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRNKA 354
Cdd:COG4372  92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
 
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 8.58e-156

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: 459.49  E-value: 8.58e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    48 EEQLPQYKLRVDSLF-LYENQDWS--QSSHQQQDASETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDR 124
Cdd:pfam04849   1 EEQIPPYKLRADTLGtGYANQDWKipSPAGRPPEVSLPLSPEQIRETLNYFLLCSDRVSQMTKTYNDIEAVTRLLEEKER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   125 DLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELSKKEELLRIVSIASEESETDSSCSTPLRFNESFSLS 204
Cdd:pfam04849  81 DLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   205 QGLLQLDMMHEKLKELEEENMALRSKACHIKTETFTYEEKEQKLINDCVNELRETNAQMSRMTEELSGKSDELLRYQEEI 284
Cdd:pfam04849 161 HGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEI 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75905813   285 SSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRNK 353
Cdd:pfam04849 241 TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
414-565 5.20e-25

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


Pssm-ID: 463588  Cd Length: 171  Bit Score: 102.36  E-value: 5.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   414 RGRSVTfPVLLPIPGSNRSSVIMTAKPFESGVQQT------------EDKTLPN--QGSSTEVPGNSHPRDP--PGLPED 477
Cdd:pfam12448   1 RQRSLT-PSPMNIPGSNQSSSLTSMRSSSSSTPRSsyyggdgssislDNRTNSIlsETSSSQDSGYDRPKKPgtPGTPGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   478 SDLATALHRLSLRRQNYLSEKQFFAEEWERKLQILAEQE--EEVSSCEALT--ENLASFCTDQSETTELGSAGCLRGFMP 553
Cdd:pfam12448  80 RDLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGTYnyDEGEHGGSLTpnDSIMSLGSNHSGSSSHSSGFSSRSYLP 159
                         170
                  ....*....|..
gi 75905813   554 EKLQIVKPLEGS 565
Cdd:pfam12448 160 EKLQIVKPLEGS 171
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
255-353 2.52e-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: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813   255 ELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEElrlhlqasKDAQRQLtmELHELQDRNM 334
Cdd:pfam06785  91 TLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE--------QLAEKQL--LINEYQQTIE 160
                          90
                  ....*....|....*....
gi 75905813   335 ECLGMLHESQEEIKELRNK 353
Cdd:pfam06785 161 EQRSVLEKRQDQIENLESK 179
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
244-351 7.63e-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: 42.70  E-value: 7.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    244 KEQKLINDCVNELRETNAQMSRMTEEL--------SGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQAS 315
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLkqledeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 75905813    316 KDAQRQLTMELHELQDRNMECLGMlheSQEEIKELR 351
Cdd:smart00787 245 TNKKSELNTEIAEAEKKLEQCRGF---TFKEIEKLK 277
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
102-428 1.07e-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: 43.12  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    102 VEQMTKTYNDIDMVTHLLAE-RDRDLELAARIgQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELSKKEELLRIVSI 180
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEElRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    181 ASEESETDSSCSTplrfNESFSLSQGLLQLDMMHEKLKELEEeNMALRSKACHIKTETFtyeekeQKLINDCVNELRETN 260
Cdd:TIGR02168  331 KLDELAEELAELE----EKLEELKEELESLEAELEELEAELE-ELESRLEELEEQLETL------RSKVAQLELQIASLN 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    261 AQMSRMTEELSGKSDELLRYQEEISSLLSQ-------------------IVDLQHKLKEHVIEKEELRLHLQASKDAQRQ 321
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKleeaelkelqaeleeleeeLEELQEELERLEEALEELREELEEAEQALDA 479
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    322 LTMELHELQDRNMECLGML--HES-QEEIKEL-RNKAGPSAHL-CFSQAYGVFAGESLAAEI--EGTMRKKLSLDEESVF 394
Cdd:TIGR02168  480 AERELAQLQARLDSLERLQenLEGfSEGVKALlKNQSGLSGILgVLSELISVDEGYEAAIEAalGGRLQAVVVENLNAAK 559
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 75905813    395 ------KQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPG 428
Cdd:TIGR02168  560 kaiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
119-353 1.32e-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: 42.74  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    119 LAERDRDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHEL----SKKEELLRIVSIASEESETDSSCSTP 194
Cdd:TIGR02168  728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeaeAEIEELEAQIEQLKEELKALREALDE 807
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    195 LRfNESFSLSQGLLQLdmmheklkeLEEENMALRSKACHIKTETFTYEEKEQKL--INDCVNELRETNAQMSRMTEELSG 272
Cdd:TIGR02168  808 LR-AELTLLNEEAANL---------RERLESLERRIAATERRLEDLEEQIEELSedIESLAAEIEELEELIEELESELEA 877
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    273 KSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHE----SQEEIK 348
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeyslTLEEAE 957

                   ....*
gi 75905813    349 ELRNK 353
Cdd:TIGR02168  958 ALENK 962
46 PHA02562
endonuclease subunit; Provisional
233-354 1.86e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813  233 HIKTETFTYeekeqkliNDCVNELRETNAQMsrmTEELSGKSDELLryqEEISSLLSQIVDLQHKLKEHVIEKEELRLHL 312
Cdd:PHA02562 192 HIQQQIKTY--------NKNIEEQRKKNGEN---IARKQNKYDELV---EEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 75905813  313 QASKDAQRQLTMELHELQ-DRNM--------ECLGMLHESQEEIKELRNKA 354
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQkVIKMyekggvcpTCTQQISEGPDRITKIKDKL 308
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
235-354 2.17e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813 235 KTETFTYEEKEQKLINDCVNELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQA 314
Cdd:COG4372  12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 75905813 315 SKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRNKA 354
Cdd:COG4372  92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
243-354 2.18e-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: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813 243 EKEQKLINDCVNELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQL 322
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
                        90       100       110
                ....*....|....*....|....*....|..
gi 75905813 323 TMELHELQDRNMECLGMLHESQEEIKELRNKA 354
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAEL 360
COG5022 COG5022
Myosin heavy chain [General function prediction only];
124-503 2.61e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813  124 RDLELAARIGQALLKRNHVLSEQNESLEEQ----LGQAFDQVNQLQHELSKKEELlRIVSIASEESETDSSCST-PLRFN 198
Cdd:COG5022  843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQsaqrVELAERQLQELKIDVKSISSL-KLVNLELESEIIELKKSLsSDLIE 921
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813  199 ESFSLSQGLLQLdmmheklkeleeenmalrskACHIKTETFtyeeKEQKLIN----DCVNELRETNAQMSRMTEELSGKS 274
Cdd:COG5022  922 NLEFKTELIARL--------------------KKLLNNIDL----EEGPSIEyvklPELNKLHEVESKLKETSEEYEDLL 977
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813  275 DELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTmELHELQDRNMECLGMLHeSQEEIKELRNKA 354
Cdd:COG5022  978 KKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVA-ELQSASKIISSESTELS-ILKPLQKLKGLL 1055
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813  355 gpsahlcfSQAYGVFAGESLAAEIegtmRKKLSLDEEsvfKQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPgsnrSSV 434
Cdd:COG5022 1056 --------LLENNQLQARYKALKL----RRENSLLDD---KQLYQLESTENLLKTINVKDLEVTNRNLVKPAN----VLQ 1116
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75905813  435 IMTAKPFESGVQQTEDKTLPNQGSSTEVPGNSHPRDPPGLPEDSDLATALHRLSLRRQNYLSEKQFFAE 503
Cdd:COG5022 1117 FIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQS 1185
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
112-355 3.11e-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: 41.58  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    112 IDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELSKKEEllRIVSIASEESETDSSC 191
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA--EIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    192 STPLRfnESFSLSQGLLQLdmmheklkeleeenmalrSKACHIKTETFTYEEKEQKLINDCVNELRETnaqMSRMTEELS 271
Cdd:TIGR02168  778 AEAEA--EIEELEAQIEQL------------------KEELKALREALDELRAELTLLNEEAANLRER---LESLERRIA 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    272 GKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRnmeclgmLHESQEEIKELR 351
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE-------LEELSEELRELE 907

                   ....
gi 75905813    352 NKAG 355
Cdd:TIGR02168  908 SKRS 911
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
119-370 4.71e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 4.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813 119 LAERDRDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELSKKEELLRIVSIASEESETDSScstplrfN 198
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-------A 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813 199 ESFSLSQGLLQLDMMHEKLKEleeeNMALRSkachiktETFTYEEKEQKLINDCVNELRETNAQMSRMTEELSGKSDELL 278
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPL----ALLLSP-------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813 279 RYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQltmELHELQDRNMECLGMLHESQEEIKELRNKAGPSA 358
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
                       250
                ....*....|..
gi 75905813 359 hlcFSQAYGVFA 370
Cdd:COG4942 248 ---FAALKGKLP 256
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
242-398 7.75e-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: 40.05  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75905813    242 EEKEQKLiNDCVNELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQ 321
Cdd:TIGR02169  311 AEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75905813    322 LTMELHELQDRNMECLGMLHESQEEIKELRNKagpsahlcfsqaygvfaGESLAAEIEGTMRKKLSLDEESVFKQKA 398
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEE-----------------LADLNAAIAGIEAKINELEEEKEDKALE 449
 
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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