NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530425257|ref|XP_005259622|]
View 

paralemmin-1 isoform X1 [Homo sapiens]

Protein Classification

Paralemmin domain-containing protein( domain architecture ID 10505538)

Paralemmin domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
21-351 9.17e-118

Paralemmin;


:

Pssm-ID: 460875  Cd Length: 301  Bit Score: 344.04  E-value: 9.17e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257   21 AEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVL 100
Cdd:pfam03285   1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  101 ERGDSAPATaKENAAAPSPvrapapspakeerktevvmnsqqtpvgtpkdkrvsntplrtvdgspmmkaamysvEITVEK 180
Cdd:pfam03285  81 EEESSISAK-KENLAEKLL-------------------------------------------------------EITVEK 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  181 DKVTGETRVLSSTTLLPRQPLPLGIKVYEDETKVVHAV---DGTAENGIHPLSSSEVDELIHKADEVTLSEAGSTAGAAE 257
Cdd:pfam03285 105 DKVTGETRVLSSTTLLPDDVQPQGVKVYDDETKVVHEVsggDGTEENGVHPLSSSEVEELIHKADEVTLGEGGSTAAPEV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  258 T----RGAVEGAARTTPSRR------------EITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETKKVLG 321
Cdd:pfam03285 185 RgtadGGDVSPKEEMTPKRAklemvhkprkdhEITGVEAQPGETTSEPPGAAASAEPPVTMIFMGYQNVEDEEETKKVLG 264
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 530425257  322 LQDTITAELVVIEDAAEPKEPA-------PPNGSAAE 351
Cdd:pfam03285 265 LETTIKAELVVIEDDEEKLREKtvtddstIPNGAAAE 301
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
21-351 9.17e-118

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 344.04  E-value: 9.17e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257   21 AEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVL 100
Cdd:pfam03285   1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  101 ERGDSAPATaKENAAAPSPvrapapspakeerktevvmnsqqtpvgtpkdkrvsntplrtvdgspmmkaamysvEITVEK 180
Cdd:pfam03285  81 EEESSISAK-KENLAEKLL-------------------------------------------------------EITVEK 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  181 DKVTGETRVLSSTTLLPRQPLPLGIKVYEDETKVVHAV---DGTAENGIHPLSSSEVDELIHKADEVTLSEAGSTAGAAE 257
Cdd:pfam03285 105 DKVTGETRVLSSTTLLPDDVQPQGVKVYDDETKVVHEVsggDGTEENGVHPLSSSEVEELIHKADEVTLGEGGSTAAPEV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  258 T----RGAVEGAARTTPSRR------------EITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETKKVLG 321
Cdd:pfam03285 185 RgtadGGDVSPKEEMTPKRAklemvhkprkdhEITGVEAQPGETTSEPPGAAASAEPPVTMIFMGYQNVEDEEETKKVLG 264
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 530425257  322 LQDTITAELVVIEDAAEPKEPA-------PPNGSAAE 351
Cdd:pfam03285 265 LETTIKAELVVIEDDEEKLREKtvtddstIPNGAAAE 301
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
14-129 1.13e-06

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: 50.15  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  14 QERLQAIAEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRL 93
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530425257  94 EKEIEVLERgDSAPATAKENAAAPSPVRAPAPSPAK 129
Cdd:COG4942  226 EALIARLEA-EAAAAAERTPAAGFAALKGKLPWPVS 260
rne PRK10811
ribonuclease E; Reviewed
5-382 1.39e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 44.26  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257    5 VLAAETTSQQERLQaiaEKRKRQaeienKRRQleDERRQLQhLKSKALRErwllEGTPSSASEGDEDL-----RRQMQDD 79
Cdd:PRK10811  661 VTEKARTQDEQQQA---PRRERQ-----RRRN--DEKRQAQ-QEAKALNV----EEQSVQETEQEERVqqvqpRRKQRQL 725
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257   80 EQKTRlLEDSVSRLEKEIEVLERGDSAPATAKENAAAPSPVRAPAPSPAKEERKTEVVMNSQ-QTPVGTPKDKRVSNTPL 158
Cdd:PRK10811  726 NQKVR-IEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAEnRDNNGMPRRSRRSPRHL 804
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  159 RtvdgspmmkaamysveitvekdkVTGETRVLSSTTLLPRQ-PLPLGIKVYEDETK-----VVHAVDGTAENGIHPLSSS 232
Cdd:PRK10811  805 R-----------------------VSGQRRRRYRDERYPTQsPMPLTVACASPEMAsgkvwIRYPVVRPQDVQVEEQREA 861
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  233 EVDELIHKADEVTLSEAGSTAGAAETRGAVEGAARTTPSRREITGVQAQPGEATSGPPGIQP-GQEPPVTMIFMGYQNVE 311
Cdd:PRK10811  862 EEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPvTEQPQVITESDVAVAQE 941
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425257  312 DEAETKKVLGLQDTITAELVVIEDAAEPKEPAPPNGSAAEPPT---EAASREENQAGPEATTSDPQDLDMKKHR 382
Cdd:PRK10811  942 VAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVaevAAEVETVTAVEPEVAPAQVPEATVEHNH 1015
DDRRRQL_YjdP NF041443
DDRRRQL repeat protein YjdP; Members of this family average 108 amino acids in length, with a ...
24-82 7.37e-04

DDRRRQL repeat protein YjdP; Members of this family average 108 amino acids in length, with a signal peptide and with a highly charged C-terminal region of typically five tandem 7-mer repeats approximated by DDRRRQL. The family is named for founding member YjdP from Escherichia coli K-12.


Pssm-ID: 469333 [Multi-domain]  Cd Length: 102  Bit Score: 38.43  E-value: 7.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530425257  24 RKRQaeIENKRRQLEDERRQLQHlkskalRERWLlegtpssasegDEDlRRQMQDDEQK 82
Cdd:NF041443  63 RRRQ--YDDRRRQLEDRRRQLDD------RQRQL-----------DQE-RRQLEDEERR 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
8-102 2.10e-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: 40.44  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257     8 AETTSQQERLQ-AIAEKRKRQAEIENKRRQLEDERRQLQ--------HLKSKALRERWLLEGTPSSASEgDEDLRRQMQD 78
Cdd:TIGR02169  297 GELEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLaeieelerEIEEERKRRDKLTEEYAELKEE-LEDLRAELEE 375
                           90       100
                   ....*....|....*....|....
gi 530425257    79 DEQKTRLLEDSVSRLEKEIEVLER 102
Cdd:TIGR02169  376 VDKEFAETRDELKDYREKLEKLKR 399
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
21-351 9.17e-118

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 344.04  E-value: 9.17e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257   21 AEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVL 100
Cdd:pfam03285   1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  101 ERGDSAPATaKENAAAPSPvrapapspakeerktevvmnsqqtpvgtpkdkrvsntplrtvdgspmmkaamysvEITVEK 180
Cdd:pfam03285  81 EEESSISAK-KENLAEKLL-------------------------------------------------------EITVEK 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  181 DKVTGETRVLSSTTLLPRQPLPLGIKVYEDETKVVHAV---DGTAENGIHPLSSSEVDELIHKADEVTLSEAGSTAGAAE 257
Cdd:pfam03285 105 DKVTGETRVLSSTTLLPDDVQPQGVKVYDDETKVVHEVsggDGTEENGVHPLSSSEVEELIHKADEVTLGEGGSTAAPEV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  258 T----RGAVEGAARTTPSRR------------EITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETKKVLG 321
Cdd:pfam03285 185 RgtadGGDVSPKEEMTPKRAklemvhkprkdhEITGVEAQPGETTSEPPGAAASAEPPVTMIFMGYQNVEDEEETKKVLG 264
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 530425257  322 LQDTITAELVVIEDAAEPKEPA-------PPNGSAAE 351
Cdd:pfam03285 265 LETTIKAELVVIEDDEEKLREKtvtddstIPNGAAAE 301
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
14-129 1.13e-06

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: 50.15  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  14 QERLQAIAEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRL 93
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530425257  94 EKEIEVLERgDSAPATAKENAAAPSPVRAPAPSPAK 129
Cdd:COG4942  226 EALIARLEA-EAAAAAERTPAAGFAALKGKLPWPVS 260
rne PRK10811
ribonuclease E; Reviewed
5-382 1.39e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 44.26  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257    5 VLAAETTSQQERLQaiaEKRKRQaeienKRRQleDERRQLQhLKSKALRErwllEGTPSSASEGDEDL-----RRQMQDD 79
Cdd:PRK10811  661 VTEKARTQDEQQQA---PRRERQ-----RRRN--DEKRQAQ-QEAKALNV----EEQSVQETEQEERVqqvqpRRKQRQL 725
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257   80 EQKTRlLEDSVSRLEKEIEVLERGDSAPATAKENAAAPSPVRAPAPSPAKEERKTEVVMNSQ-QTPVGTPKDKRVSNTPL 158
Cdd:PRK10811  726 NQKVR-IEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAEnRDNNGMPRRSRRSPRHL 804
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  159 RtvdgspmmkaamysveitvekdkVTGETRVLSSTTLLPRQ-PLPLGIKVYEDETK-----VVHAVDGTAENGIHPLSSS 232
Cdd:PRK10811  805 R-----------------------VSGQRRRRYRDERYPTQsPMPLTVACASPEMAsgkvwIRYPVVRPQDVQVEEQREA 861
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257  233 EVDELIHKADEVTLSEAGSTAGAAETRGAVEGAARTTPSRREITGVQAQPGEATSGPPGIQP-GQEPPVTMIFMGYQNVE 311
Cdd:PRK10811  862 EEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPvTEQPQVITESDVAVAQE 941
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425257  312 DEAETKKVLGLQDTITAELVVIEDAAEPKEPAPPNGSAAEPPT---EAASREENQAGPEATTSDPQDLDMKKHR 382
Cdd:PRK10811  942 VAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVaevAAEVETVTAVEPEVAPAQVPEATVEHNH 1015
DDRRRQL_YjdP NF041443
DDRRRQL repeat protein YjdP; Members of this family average 108 amino acids in length, with a ...
24-82 7.37e-04

DDRRRQL repeat protein YjdP; Members of this family average 108 amino acids in length, with a signal peptide and with a highly charged C-terminal region of typically five tandem 7-mer repeats approximated by DDRRRQL. The family is named for founding member YjdP from Escherichia coli K-12.


Pssm-ID: 469333 [Multi-domain]  Cd Length: 102  Bit Score: 38.43  E-value: 7.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530425257  24 RKRQaeIENKRRQLEDERRQLQHlkskalRERWLlegtpssasegDEDlRRQMQDDEQK 82
Cdd:NF041443  63 RRRQ--YDDRRRQLEDRRRQLDD------RQRQL-----------DQE-RRQLEDEERR 101
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
4-121 1.08e-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: 40.90  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257   4 RVLAAETTSQQERLQAI-AEKRKRQAEIENKRRQLEDERRQLQHLKSKalRERwLLEGTPSSASEgdedLRRQMQDDEQK 82
Cdd:COG4942  149 REQAEELRADLAELAALrAELEAERAELEALLAELEEERAALEALKAE--RQK-LLARLEKELAE----LAAELAELQQE 221
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530425257  83 TRLLEDSVSRLEKEIEVLERGDSAPATAKENAAAPSPVR 121
Cdd:COG4942  222 AEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWPVS 260
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
8-102 2.10e-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: 40.44  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257     8 AETTSQQERLQ-AIAEKRKRQAEIENKRRQLEDERRQLQ--------HLKSKALRERWLLEGTPSSASEgDEDLRRQMQD 78
Cdd:TIGR02169  297 GELEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLaeieelerEIEEERKRRDKLTEEYAELKEE-LEDLRAELEE 375
                           90       100
                   ....*....|....*....|....
gi 530425257    79 DEQKTRLLEDSVSRLEKEIEVLER 102
Cdd:TIGR02169  376 VDKEFAETRDELKDYREKLEKLKR 399
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-116 3.04e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257   2 LPRVLAAETTSQQERLQAIAEKRKRQAEIENKRRQLEDERRQLQHLKSKALRErwllegtpssASEGDEDLRRQMQDDEQ 81
Cdd:COG4717  144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAEELEELQQRLAELEE 213
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530425257  82 KTRLLEDSVSRLEKEIEVLERGDSAPATAKENAAA 116
Cdd:COG4717  214 ELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3-130 7.23e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.51  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425257     3 PRVLAAETTSQQERLQAIAEK-----------RKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDED 71
Cdd:TIGR02169  662 PRGGILFSRSEPAELQRLRERleglkrelsslQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 530425257    72 LRRQMQDDEQKTRLLEDSVSRLEKEIEVLERgdsapATAKENAAAPSPVRAPAPSPAKE 130
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEE-----DLHKLEEALNDLEARLSHSRIPE 795
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
14-87 7.70e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.57  E-value: 7.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425257   14 QERLQAIAEKRKRQAEIENKRRQLE-DERRQLQHLKSKALRERWLLEgtpssASEGDEDLRRQMQDDEQKTRLLE 87
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLE-----AMEREREMMRQIVESEKARAEYE 592
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH