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Conserved domains on  [gi|48374087|ref|NP_853659|]
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tumor susceptibility gene 101 protein [Rattus norvegicus]

Protein Classification

UEV and Vps23_core domain-containing protein( domain architecture ID 10530391)

UEV and Vps23_core domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-139 3.57e-66

UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other human malignancies. However, the involvement of this gene in neoplastic transformation and tumorigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but that this gene is not a tumour suppressor for sporadic forms of breast cancer. This family is related to the ubiquitin conjugating enzymes.


:

Pssm-ID: 399041  Cd Length: 119  Bit Score: 205.96  E-value: 3.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087    21 TVRQTVNVIAMYKDLKPVLDSYVFNDGSSRELVNLTGTIPVRYRGNIYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 48374087   101 KHVDANGKIYLPYLHDWKHPRSELLELIQIMIVIFGEEP 139
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQEDP 119
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 317-376 2.57e-28

Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. The core domain of the Vps23 subunit of the heterotrimeric ESCRT-I complex is a helical hairpin sandwiched in a fan-like formation between two other helical hairpins from Vps28 (pfam03997) and Vps37. Vps23 gives ESCRT-I complex its stability.


:

Pssm-ID: 462803 [Multi-domain]  Cd Length: 60  Bit Score: 105.24  E-value: 2.57e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087   317 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 376
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
229-350 2.07e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 229 ASLISAVSDKLRwRMKEEMDGAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDE 297
Cdd:COG4372  23 GILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 48374087 298 ELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 350
Cdd:COG4372 102 ELESLQEEAEELQE--ELEELQ-------KERQDLEQQRKQLEAQIAELQSEI 145
 
Name Accession Description Interval E-value
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-139 3.57e-66

UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other human malignancies. However, the involvement of this gene in neoplastic transformation and tumorigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but that this gene is not a tumour suppressor for sporadic forms of breast cancer. This family is related to the ubiquitin conjugating enzymes.


Pssm-ID: 399041  Cd Length: 119  Bit Score: 205.96  E-value: 3.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087    21 TVRQTVNVIAMYKDLKPVLDSYVFNDGSSRELVNLTGTIPVRYRGNIYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 48374087   101 KHVDANGKIYLPYLHDWKHPRSELLELIQIMIVIFGEEP 139
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQEDP 119
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 19-143 1.57e-61

ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the UEV domain of eukaryotic tumor susceptibility gene 101 protein (TSG101, also known as ESCRT-I complex subunit TSG101, vacuolar protein-sorting protein 23, or Vps23) which functions in endocytic trafficking. TSG101 is a component of the ESCRT (endosomal sorting complex required for transport)-I complex, one of four complexes (ESCRT 0, -I, -II, -III) in the vacuolar protein sorting pathway. TSG101 also facilitates HIV-1 virus budding from infected cells, perhaps by linking the p6 domain of the viral structural Gag protein to the vacuolar protein sorting machinery. The UEV domain of TSG101 binds to an essential tetrapeptide motif within the p6 domain of the structural Gag protein and also to ubiquitin. UEVs are homologous to E2 ubiquitin ligases but lack the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467408  Cd Length: 126  Bit Score: 194.06  E-value: 1.57e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087  19 DLTVRQTVNVIAMYKDLKPVLDSYVFNDGSSRELVNLTGTIPVRYRGNIYNIPICLWLLDTYPYNPPICFVKPTSSMTI- 97
Cdd:cd11685   1 DRVREDLLNLLQKYPSLKPKTDTFTFNDGSSKLLLCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMIi 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 48374087  98 KTGKHVDANGKIYLPYLHDWKHPRSELLELIQIMIVIFGEEPPVFS 143
Cdd:cd11685  81 KPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 317-376 2.57e-28

Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. The core domain of the Vps23 subunit of the heterotrimeric ESCRT-I complex is a helical hairpin sandwiched in a fan-like formation between two other helical hairpins from Vps28 (pfam03997) and Vps37. Vps23 gives ESCRT-I complex its stability.


Pssm-ID: 462803 [Multi-domain]  Cd Length: 60  Bit Score: 105.24  E-value: 2.57e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087   317 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 376
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 23-149 2.87e-13

Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologues. This pathway functions in regulating many fundamental processes required for cell viability.TSG101 is one of several UBC homologues that lacks this active site cysteine.


Pssm-ID: 214562 [Multi-domain]  Cd Length: 145  Bit Score: 66.55  E-value: 2.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087     23 RQTVNVIAMYKDLKPVLDSYVFNDGSSREL-VNLTGTIPVRYRGNIYniPICLWLLDTYPYNPPICFVKPTssmtiKTGK 101
Cdd:smart00212   1 RLLKELKELRKDPPPGFTAYPVDDENLLEWtGTIVGPPGTPYEGGVF--KLTIEFPEDYPFKPPKVKFITK-----IYHP 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 48374087    102 HVDANGKIYLPYLH--DWKHPRSelLELIQIMIVIFGEEPPVFSRPTVSA 149
Cdd:smart00212  74 NVDSSGEICLDILKqeKWSPALT--LETVLLSLQSLLSEPNPDSPLNADA 121
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
229-350 2.07e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 229 ASLISAVSDKLRwRMKEEMDGAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDE 297
Cdd:COG4372  23 GILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 48374087 298 ELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 350
Cdd:COG4372 102 ELESLQEEAEELQE--ELEELQ-------KERQDLEQQRKQLEAQIAELQSEI 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 242-384 3.05e-06

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: 49.28  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087    242 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEnndideviip 321
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE---------- 347

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48374087    322 taPLYKQILNLYAEENAIEDTIfylgEALRRGVIDLDvflKHVRLLSRKQFQLRALMQKARKT 384
Cdd:TIGR02168  348 --ELKEELESLEAELEELEAEL----EELESRLEELE---EQLETLRSKVAQLELQIASLNNE 401
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 251-314 6.10e-05

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 41.40  E-value: 6.10e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48374087 251 QAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLkkKDE------ELSSALEKMEN-QSENND 314
Cdd:cd22887   3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL--NDElialqiENNLLEEKLRKlQEENDE 71
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 237-293 6.29e-05

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 43.27  E-value: 6.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48374087   237 DKLRWRMKEEMDGAQAE----LNALK-RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLK 293
Cdd:pfam07798  89 EKLKQRLREEITKLKADvrldLNLEKgRIREELKAQELKIQETNNKIDTEIANLRTQIESVK 150
PRK10325 PRK10325
heat shock protein GrpE; Provisional
 242-307 3.62e-04

heat shock protein GrpE; Provisional


Pssm-ID: 182379 [Multi-domain]  Cd Length: 197  Bit Score: 41.20  E-value: 3.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48374087  242 RMKEEMDgaqaelNALKRTEEDLKKGHQ-KLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 307
Cdd:PRK10325  64 RVKAEME------NLRRRTELDIEKAHKfALEKFINELLPVIDSLDRALEVADKANPDMSAMVEGIE 124
 
Name Accession Description Interval E-value
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-139 3.57e-66

UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other human malignancies. However, the involvement of this gene in neoplastic transformation and tumorigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but that this gene is not a tumour suppressor for sporadic forms of breast cancer. This family is related to the ubiquitin conjugating enzymes.


Pssm-ID: 399041  Cd Length: 119  Bit Score: 205.96  E-value: 3.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087    21 TVRQTVNVIAMYKDLKPVLDSYVFNDGSSRELVNLTGTIPVRYRGNIYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 48374087   101 KHVDANGKIYLPYLHDWKHPRSELLELIQIMIVIFGEEP 139
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQEDP 119
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 19-143 1.57e-61

ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the UEV domain of eukaryotic tumor susceptibility gene 101 protein (TSG101, also known as ESCRT-I complex subunit TSG101, vacuolar protein-sorting protein 23, or Vps23) which functions in endocytic trafficking. TSG101 is a component of the ESCRT (endosomal sorting complex required for transport)-I complex, one of four complexes (ESCRT 0, -I, -II, -III) in the vacuolar protein sorting pathway. TSG101 also facilitates HIV-1 virus budding from infected cells, perhaps by linking the p6 domain of the viral structural Gag protein to the vacuolar protein sorting machinery. The UEV domain of TSG101 binds to an essential tetrapeptide motif within the p6 domain of the structural Gag protein and also to ubiquitin. UEVs are homologous to E2 ubiquitin ligases but lack the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467408  Cd Length: 126  Bit Score: 194.06  E-value: 1.57e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087  19 DLTVRQTVNVIAMYKDLKPVLDSYVFNDGSSRELVNLTGTIPVRYRGNIYNIPICLWLLDTYPYNPPICFVKPTSSMTI- 97
Cdd:cd11685   1 DRVREDLLNLLQKYPSLKPKTDTFTFNDGSSKLLLCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMIi 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 48374087  98 KTGKHVDANGKIYLPYLHDWKHPRSELLELIQIMIVIFGEEPPVFS 143
Cdd:cd11685  81 KPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 317-376 2.57e-28

Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. The core domain of the Vps23 subunit of the heterotrimeric ESCRT-I complex is a helical hairpin sandwiched in a fan-like formation between two other helical hairpins from Vps28 (pfam03997) and Vps37. Vps23 gives ESCRT-I complex its stability.


Pssm-ID: 462803 [Multi-domain]  Cd Length: 60  Bit Score: 105.24  E-value: 2.57e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087   317 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 376
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 23-149 2.87e-13

Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologues. This pathway functions in regulating many fundamental processes required for cell viability.TSG101 is one of several UBC homologues that lacks this active site cysteine.


Pssm-ID: 214562 [Multi-domain]  Cd Length: 145  Bit Score: 66.55  E-value: 2.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087     23 RQTVNVIAMYKDLKPVLDSYVFNDGSSREL-VNLTGTIPVRYRGNIYniPICLWLLDTYPYNPPICFVKPTssmtiKTGK 101
Cdd:smart00212   1 RLLKELKELRKDPPPGFTAYPVDDENLLEWtGTIVGPPGTPYEGGVF--KLTIEFPEDYPFKPPKVKFITK-----IYHP 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 48374087    102 HVDANGKIYLPYLH--DWKHPRSelLELIQIMIVIFGEEPPVFSRPTVSA 149
Cdd:smart00212  74 NVDSSGEICLDILKqeKWSPALT--LETVLLSLQSLLSEPNPDSPLNADA 121
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
229-350 2.07e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 229 ASLISAVSDKLRwRMKEEMDGAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDE 297
Cdd:COG4372  23 GILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 48374087 298 ELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 350
Cdd:COG4372 102 ELESLQEEAEELQE--ELEELQ-------KERQDLEQQRKQLEAQIAELQSEI 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 242-384 3.05e-06

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: 49.28  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087    242 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEnndideviip 321
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE---------- 347

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48374087    322 taPLYKQILNLYAEENAIEDTIfylgEALRRGVIDLDvflKHVRLLSRKQFQLRALMQKARKT 384
Cdd:TIGR02168  348 --ELKEELESLEAELEELEAEL----EELESRLEELE---EQLETLRSKVAQLELQIASLNNE 401
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
242-370 7.62e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 7.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 242 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIP 321
Cdd:COG4372  98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 48374087 322 TAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRK 370
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-383 4.66e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 4.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087    244 KEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKK----DEELSSALEKMENQSEN------- 312
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEieellkk 429

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48374087    313 ---NDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARK 383
Cdd:TIGR02168  430 leeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 251-314 6.10e-05

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 41.40  E-value: 6.10e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48374087 251 QAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLkkKDE------ELSSALEKMEN-QSENND 314
Cdd:cd22887   3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL--NDElialqiENNLLEEKLRKlQEENDE 71
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 237-293 6.29e-05

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 43.27  E-value: 6.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48374087   237 DKLRWRMKEEMDGAQAE----LNALK-RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLK 293
Cdd:pfam07798  89 EKLKQRLREEITKLKADvrldLNLEKgRIREELKAQELKIQETNNKIDTEIANLRTQIESVK 150
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 231-343 9.66e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.63  E-value: 9.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087   231 LISAVSDKLRWRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMEnqS 310
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK--K 624

                          90       100       110
                  ....*....|....*....|....*....|...
gi 48374087   311 ENNDIDEvIIPTAPLYKQILNLYAEenAIEDTI 343
Cdd:TIGR04523 625 ENEKLSS-IIKNIKSKKNKLKQEVK--QIKETI 654
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 232-305 1.77e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 1.77e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48374087 232 ISAVSDKLRwRMKEEMDGAQAELNALKRTEEDLKKghqKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEK 305
Cdd:COG1579 105 ISDLEDEIL-ELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
PRK10325 PRK10325
heat shock protein GrpE; Provisional
 242-307 3.62e-04

heat shock protein GrpE; Provisional


Pssm-ID: 182379 [Multi-domain]  Cd Length: 197  Bit Score: 41.20  E-value: 3.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48374087  242 RMKEEMDgaqaelNALKRTEEDLKKGHQ-KLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 307
Cdd:PRK10325  64 RVKAEME------NLRRRTELDIEKAHKfALEKFINELLPVIDSLDRALEVADKANPDMSAMVEGIE 124
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
245-312 5.39e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 5.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48374087  245 EEMDGAQAELNALKRTEEDLKKG-----HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 312
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 225-370 5.74e-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: 41.98  E-value: 5.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087    225 DTIRASLiSAVSDKLRwRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALE 304
Cdd:TIGR02169  794 PEIQAEL-SKLEEEVS-RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 48374087    305 KMENQsenndIDEVIIPTAPLYKQILNLYAEENAIEDtifylgealRRGVIDLDVFLKHVRLLSRK 370
Cdd:TIGR02169  872 ELEAA-----LRDLESRLGDLKKERDELEAQLRELER---------KIEELEAQIEKKRKRLSELK 923
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 232-343 6.32e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 6.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 232 ISAVSDKLRwRMKEEMDGAQA--ELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALE--KME 307
Cdd:COG1579  68 IEEVEARIK-KYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEekKAE 146

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 48374087 308 NQSENNDIDeviiptaplyKQILNLYAEENAIEDTI 343
Cdd:COG1579 147 LDEELAELE----------AELEELEAEREELAAKI 172
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 230-306 7.25e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 7.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48374087 230 SLISAVSDKLRwRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKM 306
Cdd:COG3883  16 PQIQAKQKELS-ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 244-314 1.33e-03

Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain


Pssm-ID: 238105 [Multi-domain]  Cd Length: 151  Bit Score: 38.80  E-value: 1.33e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48374087 244 KEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENND 314
Cdd:cd00179  12 RGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSSV 82
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 228-311 2.36e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 2.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 228 RASLISAVSDKLRwRMKEEMDGAQAELNALKR----TEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSAL 303
Cdd:COG3883 120 RLSALSKIADADA-DLLEELKADKAELEAKKAeleaKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198


                ....*...
gi 48374087 304 EKMENQSE 311
Cdd:COG3883 199 AELEAELA 206
PHA03369 PHA03369
capsid maturational protease; Provisional
 147-324 2.38e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 39.98  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087  147 VSASYPPYTAAGPPNTSYLPSM---PSGISAYPSGYPP--NPSGYPgcpYPPAGPYPATTSSQYPSQPPVTTAGPSRDGT 221
Cdd:PHA03369 359 VLAAAAKVAVIAAPQTHTGPADrqrPQRPDGIPYSVPArsPMTAYP---PVPQFCGDPGLVSPYNPQSPGTSYGPEPVGP 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087  222 ISEDTirasliSAVSDklrwrMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEvdknielLKKKDEELSS 301
Cdd:PHA03369 436 VPPQP------TNPYV-----MPISMANMVYPGHPQEHGHERKRKRGGELKEELIETLKLVKK-------LKEEQESLAK 497

                        170       180
                 ....*....|....*....|...
gi 48374087  302 ALEKMENQSENNDIDEVIIPTAP 324
Cdd:PHA03369 498 ELEATAHKSEIKKIAESEFKNAG 520
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
228-383 2.41e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087  228 RASLISAVSDkLRWRMKEeMDGAQAELNALKRTEEDLKKGHQKLEEmvtrLDQEVAEVDKNIELLKKKDEELSSALEKME 307
Cdd:COG4913  646 RREALQRLAE-YSWDEID-VASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLE 719

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087  308 NQSENndideviiptapLYKQILNLYAEENAIEDTI----FYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARK 383
Cdd:COG4913  720 KELEQ------------AEEELDELQDRLEAAEDLArlelRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
PRK12704 PRK12704
phosphodiesterase; Provisional
 244-312 2.54e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 2.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087  244 KEEMDGAQAELNALKR-TEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 312
Cdd:PRK12704  56 KEALLEAKEEIHKLRNeFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
PRK10698 PRK10698
phage shock protein PspA; Provisional
 224-303 2.67e-03

phage shock protein PspA; Provisional


Pssm-ID: 182657 [Multi-domain]  Cd Length: 222  Bit Score: 38.99  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087  224 EDT---IRASLISAVSDKLRWRMKEEMDGAQ-------AELnALKRTEEDLKKG----HQKLEEMVTRLDQEVAEVDKNI 289
Cdd:PRK10698  37 EDTlveVRSTSARALAEKKQLTRRIEQAEAQqvewqekAEL-ALRKEKEDLARAalieKQKLTDLIATLEHEVTLVDETL 115

                         90
                 ....*....|....
gi 48374087  290 ELLKKKDEELSSAL 303
Cdd:PRK10698 116 ARMKKEIGELENKL 129
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 237-311 2.70e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.59  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087   237 DKLRwRMKEEMDGAQAELNA-----------LKRTEED---LKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSA 302
Cdd:pfam20492  13 ERLK-QYEEETKKAQEELEEseetaeeleeeRRQAEEEaerLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE 91


                  ....*....
gi 48374087   303 LEKMENQSE 311
Cdd:pfam20492  92 IARLEEEVE 100
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
242-352 3.56e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087  242 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEViip 321
Cdd:COG4913  675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL--- 751

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 48374087  322 tAPLYKQIL----------NLYAEENAIEDTIFYLGEALRR 352
Cdd:COG4913  752 -EERFAAALgdaverelreNLEERIDALRARLNRAEEELER 791
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
237-307 3.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 3.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48374087  237 DKLRwRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 307
Cdd:PRK03918 224 EKLE-KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 244-312 4.01e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.82  E-value: 4.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48374087   244 KEEMDGAQAELNA-LKRTEEDLKKGHQKL---EEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 312
Cdd:pfam20492   1 REEAEREKQELEErLKQYEEETKKAQEELeesEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEM 73
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 237-320 4.30e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087   237 DKLRWRMKEEMDGAQAELNALKRTEEDLKKG-------HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSalEKMENQ 309
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES--EKKEKE 537

                          90
                  ....*....|.
gi 48374087   310 SENNDIDEVII 320
Cdd:TIGR04523 538 SKISDLEDELN 548
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 248-319 5.53e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 38.16  E-value: 5.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48374087 248 DGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVA---EVDKNIELLKKKDEELSSALEKMEN--QSENNDIDEVI 319
Cdd:cd21116 112 TSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAvlnALKNQLNSLAEQIDAAIDALEKLSNdwQTLDSDIKELI 188
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
244-352 6.15e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 6.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 244 KEEMDGAQAELNALKRTEEDLKKGHQKLEEMV---------TRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN-- 312
Cdd:COG4717  94 QEELEELEEELEELEAELEELREELEKLEKLLqllplyqelEALEAELAELPERLEELEERLEELRELEEELEELEAEla 173

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 48374087 313 ---NDIDEVIIPTAPLYKQILNLYAEE-NAIEDTIFYLGEALRR 352
Cdd:COG4717 174 elqEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEE 217
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
232-379 8.50e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 8.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 232 ISAVSDKLRwRMKEEMDGAQAELNALKRTEEDLKKGHQK--------------LEEMVTRLDQEVAEVDKNIELLKKkdE 297
Cdd:COG4372 103 LESLQEEAE-ELQEELEELQKERQDLEQQRKQLEAQIAElqseiaereeelkeLEEQLESLQEELAALEQELQALSE--A 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 298 ELSSALEKMENQSENNdidEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRAL 377
Cdd:COG4372 180 EAEQALDELLKEANRN---AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256


                ..
gi 48374087 378 MQ 379
Cdd:COG4372 257 LK 258
RPN7 COG5187
26S proteasome regulatory complex component, contains PCI domain [Posttranslational ...
 265-366 9.72e-03

26S proteasome regulatory complex component, contains PCI domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227514 [Multi-domain]  Cd Length: 412  Bit Score: 37.97  E-value: 9.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48374087 265 KKGHQKLEEMVTRLDQEVAEvdkniELLKKKDE---ELSSALEKMENQSENNDIDEVIIPTAPLYKQILNLyaeENAIEd 341
Cdd:COG5187  66 EKGNPKTSASVIKFDRGRMN-----TLLKKNEEkieELDERIREKEEDNGETEGSEADRNIAEYYCQIMDI---QNGFE- 136

                        90       100
                ....*....|....*....|....*...
gi 48374087 342 tifYLGEALRRGV---IDLDVFLKHVRL 366
Cdd:COG5187 137 ---WMRRLMRDAMstgLKIDVFLCKIRL 161
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 233-301 9.75e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 36.08  E-value: 9.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48374087   233 SAVSDKLRwRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEmvtRLDQEVAEVDKNIELLKKKDEELSS 301
Cdd:pfam07926  53 AEDIKALQ-ALREELNELKAEIAELKAEAESAKAELEESEE---SWEEQKKELEKELSELEKRIEDLNE 117
 
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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