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Conserved domains on  [gi|18677765|ref|NP_570842|]
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paralemmin-1 [Rattus norvegicus]

Protein Classification

Paralemmin domain-containing protein( domain architecture ID 10505538)

Paralemmin domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
19-348 1.32e-113

Paralemmin;


:

Pssm-ID: 460875  Cd Length: 301  Bit Score: 333.25  E-value: 1.32e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765    19 AEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTPSSASEGDEDMRKQMQEDEQKARSLEESITRLEKEIDVL 98
Cdd:pfam03285   1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765    99 EFGESAPAApKENSAAPSPirphstspakeeqksetmvnaqqtplgtpkenrkstpvrspggstmmkaamysvEITVEKD 178
Cdd:pfam03285  81 EEESSISAK-KENLAEKLL------------------------------------------------------EITVEKD 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765   179 KVTGETRVLSSTTLLPRDPLPQGVKVYEDETKVVHAV---DGLSENGIQPLSSSEVDELIHKADEVTLSEAGSTTgPAEP 255
Cdd:pfam03285 106 KVTGETRVLSSTTLLPDDVQPQGVKVYDDETKVVHEVsggDGTEENGVHPLSSSEVEELIHKADEVTLGEGGSTA-APEV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765   256 RGLAEDVT-----RTTPSRR------------EITGVEAQPGEATSGPPGIQPGQEPPVTMVFMGYQNVEDEAETKKVLG 318
Cdd:pfam03285 185 RGTADGGDvspkeEMTPKRAklemvhkprkdhEITGVEAQPGETTSEPPGAAASAEPPVTMIFMGYQNVEDEEETKKVLG 264
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 18677765   319 LQDTIKAELVVIEDSVTPREPA-------PLNGSAAE 348
Cdd:pfam03285 265 LETTIKAELVVIEDDEEKLREKtvtddstIPNGAAAE 301
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
19-348 1.32e-113

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 333.25  E-value: 1.32e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765    19 AEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTPSSASEGDEDMRKQMQEDEQKARSLEESITRLEKEIDVL 98
Cdd:pfam03285   1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765    99 EFGESAPAApKENSAAPSPirphstspakeeqksetmvnaqqtplgtpkenrkstpvrspggstmmkaamysvEITVEKD 178
Cdd:pfam03285  81 EEESSISAK-KENLAEKLL------------------------------------------------------EITVEKD 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765   179 KVTGETRVLSSTTLLPRDPLPQGVKVYEDETKVVHAV---DGLSENGIQPLSSSEVDELIHKADEVTLSEAGSTTgPAEP 255
Cdd:pfam03285 106 KVTGETRVLSSTTLLPDDVQPQGVKVYDDETKVVHEVsggDGTEENGVHPLSSSEVEELIHKADEVTLGEGGSTA-APEV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765   256 RGLAEDVT-----RTTPSRR------------EITGVEAQPGEATSGPPGIQPGQEPPVTMVFMGYQNVEDEAETKKVLG 318
Cdd:pfam03285 185 RGTADGGDvspkeEMTPKRAklemvhkprkdhEITGVEAQPGETTSEPPGAAASAEPPVTMIFMGYQNVEDEEETKKVLG 264
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 18677765   319 LQDTIKAELVVIEDSVTPREPA-------PLNGSAAE 348
Cdd:pfam03285 265 LETTIKAELVVIEDDEEKLREKtvtddstIPNGAAAE 301
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
12-119 1.37e-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: 49.76  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765  12 QERLQAIAEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTPSSASEGDEDMRKQMQEDEQKARSLEESITRL 91
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
                        90       100
                ....*....|....*....|....*...
gi 18677765  92 EKEIDVLEfGESAPAAPKENSAAPSPIR 119
Cdd:COG4942 226 EALIARLE-AEAAAAAERTPAAGFAALK 252
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
19-348 1.32e-113

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 333.25  E-value: 1.32e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765    19 AEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTPSSASEGDEDMRKQMQEDEQKARSLEESITRLEKEIDVL 98
Cdd:pfam03285   1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765    99 EFGESAPAApKENSAAPSPirphstspakeeqksetmvnaqqtplgtpkenrkstpvrspggstmmkaamysvEITVEKD 178
Cdd:pfam03285  81 EEESSISAK-KENLAEKLL------------------------------------------------------EITVEKD 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765   179 KVTGETRVLSSTTLLPRDPLPQGVKVYEDETKVVHAV---DGLSENGIQPLSSSEVDELIHKADEVTLSEAGSTTgPAEP 255
Cdd:pfam03285 106 KVTGETRVLSSTTLLPDDVQPQGVKVYDDETKVVHEVsggDGTEENGVHPLSSSEVEELIHKADEVTLGEGGSTA-APEV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765   256 RGLAEDVT-----RTTPSRR------------EITGVEAQPGEATSGPPGIQPGQEPPVTMVFMGYQNVEDEAETKKVLG 318
Cdd:pfam03285 185 RGTADGGDvspkeEMTPKRAklemvhkprkdhEITGVEAQPGETTSEPPGAAASAEPPVTMIFMGYQNVEDEEETKKVLG 264
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 18677765   319 LQDTIKAELVVIEDSVTPREPA-------PLNGSAAE 348
Cdd:pfam03285 265 LETTIKAELVVIEDDEEKLREKtvtddstIPNGAAAE 301
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
12-119 1.37e-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: 49.76  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765  12 QERLQAIAEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTPSSASEGDEDMRKQMQEDEQKARSLEESITRL 91
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
                        90       100
                ....*....|....*....|....*...
gi 18677765  92 EKEIDVLEfGESAPAAPKENSAAPSPIR 119
Cdd:COG4942 226 EALIARLE-AEAAAAAERTPAAGFAALK 252
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
12-99 7.57e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 7.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765  12 QERLQAIAEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRErwllegtpssASEGDEDMRKQMQEDEQKARSLEESITRL 91
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAEELEELQQRLAELEEELEEAQEELEEL 225

                ....*...
gi 18677765  92 EKEIDVLE 99
Cdd:COG4717 226 EEELEQLE 233
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
3-171 1.19e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765   3 VLATDTVSQQERlQAIAEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTpssasegDEDMRKQMQEDEQKAR 82
Cdd:COG3883 121 LSALSKIADADA-DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ-------QAEQEALLAQLSAEEA 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765  83 SLEESITRLEKEIDVLEFGESAPAAPKENSAAPSPIRPHSTSPAKEEQKSETMVNAQQTPLGTPKENRKSTPVRSPGGST 162
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAA 272

                ....*....
gi 18677765 163 MMKAAMYSV 171
Cdd:COG3883 273 GAGAAAASA 281
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
12-98 3.39e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.77  E-value: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765     12 QERLQaiaEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTPSSASEGDEDMRKQMQEDEQKARSLEESITRL 91
Cdd:pfam01576  474 QELLQ---EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550

                   ....*..
gi 18677765     92 EKEIDVL 98
Cdd:pfam01576  551 QRELEAL 557
PrfA COG0216
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ...
7-98 9.56e-03

Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein chain release factor RF1 is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439986 [Multi-domain]  Cd Length: 356  Bit Score: 37.67  E-value: 9.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677765   7 DTVSQQERLQAIAEKRRKQAEIESKRRQLEDDRRQLQYLKSkalrerwLLEgtpssaSEGDEDMRkQMQEDEQKArsLEE 86
Cdd:COG0216  24 EVISDQKRFRKLSKEYAELEPIVEAYREYKKLLEDIEEAKE-------LLE------EESDPEMR-EMAKEELEE--LEA 87
                        90
                ....*....|..
gi 18677765  87 SITRLEKEIDVL 98
Cdd:COG0216  88 RLEELEEELKIL 99
 
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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