NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|5454140|ref|NP_006283|]
View 

tumor susceptibility gene 101 protein [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.17e-67

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: 209.42  E-value: 1.17e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140     21 TVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 5454140    101 KHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEP 139
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQEDP 119
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 316-375 2.17e-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: 105.62  E-value: 2.17e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140    316 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 375
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
211-349 1.59e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 1.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  211 TTVGPSRDGTISEDTIRASLISAVSDKLRwRMKEEMDRAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQ 279
Cdd:COG4372   6 EKVGKARLSLFGLRPKTGILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEE 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  280 EVAEVDKNIELLKKKDEELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 349
Cdd:COG4372  85 LNEQLQAAQAELAQAQEELESLQEEAEELQE--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 1.17e-67

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: 209.42  E-value: 1.17e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140     21 TVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 5454140    101 KHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEP 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 4.72e-63

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: 197.92  E-value: 4.72e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140   19 DLTVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTI- 97
Cdd:cd11685   1 DRVREDLLNLLQKYPSLKPKTDTFTFNDGSSKLLLCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMIi 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 5454140   98 KTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEPPVFS 143
Cdd:cd11685  81 KPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 316-375 2.17e-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: 105.62  E-value: 2.17e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140    316 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 375
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 23-155 1.41e-17

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: 78.88  E-value: 1.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140      23 RETVNVITLYKDLKPVLDSYVFNDGSSREL-MNLTGTIPVPYRGNTYniPICLWLLDTYPYNPPICFVKPTssmtiKTGK 101
Cdd:smart00212   1 RLLKELKELRKDPPPGFTAYPVDDENLLEWtGTIVGPPGTPYEGGVF--KLTIEFPEDYPFKPPKVKFITK-----IYHP 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 5454140     102 HVDANGKIYLPYLHE--WKhPQSDLLGLIQVmIVVFGDEPPVFSRPISASYPPYQA 155
Cdd:smart00212  74 NVDSSGEICLDILKQekWS-PALTLETVLLS-LQSLLSEPNPDSPLNADAAELYKK 127
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
211-349 1.59e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 1.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  211 TTVGPSRDGTISEDTIRASLISAVSDKLRwRMKEEMDRAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQ 279
Cdd:COG4372   6 EKVGKARLSLFGLRPKTGILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEE 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  280 EVAEVDKNIELLKKKDEELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 349
Cdd:COG4372  85 LNEQLQAAQAELAQAQEELESLQEEAEELQE--ELEELQ-------KERQDLEQQRKQLEAQIAELQSEI 145
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 236-292 7.30e-06

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: 45.97  E-value: 7.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5454140    236 DKLRWRMKEEMDRAQAE----LNALK-RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLK 292
Cdd:pfam07798  89 EKLKQRLREEITKLKADvrldLNLEKgRIREELKAQELKIQETNNKIDTEIANLRTQIESVK 150
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 238-383 1.44e-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: 47.36  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140     238 LRW-RMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSE------ 310
Cdd:TIGR02168  232 LRLeELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerl 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140     311 ---NNDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYL-----------------GEALRRGVIDLDvflKHVRLLSRKQ 370
Cdd:TIGR02168  312 anlERQLEELEAQLEELESKLDELAEELAELEEKLEELkeelesleaeleeleaeLEELESRLEELE---EQLETLRSKV 388

                          170
                   ....*....|...
gi 5454140     371 FQLRALMQKARKT 383
Cdd:TIGR02168  389 AQLELQIASLNNE 401
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 250-313 6.03e-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: 6.03e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5454140  250 QAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLkkKDE------ELSSALEKMEN-QSENND 313
Cdd:cd22887   3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL--NDElialqiENNLLEEKLRKlQEENDE 71
PRK10325 PRK10325
heat shock protein GrpE; Provisional
 241-306 1.57e-04

heat shock protein GrpE; Provisional


Pssm-ID: 182379 [Multi-domain]  Cd Length: 197  Bit Score: 42.35  E-value: 1.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5454140   241 RMKEEMDRAQAELNALKR-TEEDLKKGHQ-KLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 306
Cdd:PRK10325  57 RERDGILRVKAEMENLRRrTELDIEKAHKfALEKFINELLPVIDSLDRALEVADKANPDMSAMVEGIE 124
 
Name Accession Description Interval E-value
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-139 1.17e-67

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: 209.42  E-value: 1.17e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140     21 TVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 5454140    101 KHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEP 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 4.72e-63

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: 197.92  E-value: 4.72e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140   19 DLTVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTI- 97
Cdd:cd11685   1 DRVREDLLNLLQKYPSLKPKTDTFTFNDGSSKLLLCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMIi 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 5454140   98 KTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEPPVFS 143
Cdd:cd11685  81 KPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 316-375 2.17e-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: 105.62  E-value: 2.17e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140    316 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 375
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 23-155 1.41e-17

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: 78.88  E-value: 1.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140      23 RETVNVITLYKDLKPVLDSYVFNDGSSREL-MNLTGTIPVPYRGNTYniPICLWLLDTYPYNPPICFVKPTssmtiKTGK 101
Cdd:smart00212   1 RLLKELKELRKDPPPGFTAYPVDDENLLEWtGTIVGPPGTPYEGGVF--KLTIEFPEDYPFKPPKVKFITK-----IYHP 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 5454140     102 HVDANGKIYLPYLHE--WKhPQSDLLGLIQVmIVVFGDEPPVFSRPISASYPPYQA 155
Cdd:smart00212  74 NVDSSGEICLDILKQekWS-PALTLETVLLS-LQSLLSEPNPDSPLNADAAELYKK 127
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
211-349 1.59e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 1.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  211 TTVGPSRDGTISEDTIRASLISAVSDKLRwRMKEEMDRAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQ 279
Cdd:COG4372   6 EKVGKARLSLFGLRPKTGILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEE 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  280 EVAEVDKNIELLKKKDEELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 349
Cdd:COG4372  85 LNEQLQAAQAELAQAQEELESLQEEAEELQE--ELEELQ-------KERQDLEQQRKQLEAQIAELQSEI 145
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
241-369 1.19e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  241 RMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIP 320
Cdd:COG4372  98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5454140  321 TAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRK 369
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 236-292 7.30e-06

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: 45.97  E-value: 7.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5454140    236 DKLRWRMKEEMDRAQAE----LNALK-RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLK 292
Cdd:pfam07798  89 EKLKQRLREEITKLKADvrldLNLEKgRIREELKAQELKIQETNNKIDTEIANLRTQIESVK 150
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 238-383 1.44e-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: 47.36  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140     238 LRW-RMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSE------ 310
Cdd:TIGR02168  232 LRLeELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerl 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140     311 ---NNDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYL-----------------GEALRRGVIDLDvflKHVRLLSRKQ 370
Cdd:TIGR02168  312 anlERQLEELEAQLEELESKLDELAEELAELEEKLEELkeelesleaeleeleaeLEELESRLEELE---EQLETLRSKV 388

                          170
                   ....*....|...
gi 5454140     371 FQLRALMQKARKT 383
Cdd:TIGR02168  389 AQLELQIASLNNE 401
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 236-304 2.17e-05

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: 45.30  E-value: 2.17e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5454140  236 DKLRWRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEK 304
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 250-313 6.03e-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: 6.03e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5454140  250 QAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLkkKDE------ELSSALEKMEN-QSENND 313
Cdd:cd22887   3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL--NDElialqiENNLLEEKLRKlQEENDE 71
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-382 6.85e-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: 45.05  E-value: 6.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140     243 KEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKK----DEELSSALEKMENQSEN------- 311
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEieellkk 429

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5454140     312 ---NDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARK 382
Cdd:TIGR02168  430 leeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 243-311 7.35e-05

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: 41.83  E-value: 7.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5454140    243 KEEMDRAQAELNA-LKRTEEDLKKGHQKL---EEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 311
Cdd:pfam20492   1 REEAEREKQELEErLKQYEEETKKAQEELeesEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEM 73
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 236-310 9.01e-05

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: 41.83  E-value: 9.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140    236 DKLRwRMKEEMDRAQAELNA-----------LKRTEED---LKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSA 301
Cdd:pfam20492  13 ERLK-QYEEETKKAQEELEEseetaeeleeeRRQAEEEaerLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE 91


                  ....*....
gi 5454140    302 LEKMENQSE 310
Cdd:pfam20492  92 IARLEEEVE 100
PRK10325 PRK10325
heat shock protein GrpE; Provisional
 241-306 1.57e-04

heat shock protein GrpE; Provisional


Pssm-ID: 182379 [Multi-domain]  Cd Length: 197  Bit Score: 42.35  E-value: 1.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5454140   241 RMKEEMDRAQAELNALKR-TEEDLKKGHQ-KLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 306
Cdd:PRK10325  57 RERDGILRVKAEMENLRRrTELDIEKAHKfALEKFINELLPVIDSLDRALEVADKANPDMSAMVEGIE 124
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
244-361 2.90e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140   244 EEMDRAQAELNALKRTEEDLKKG-----HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENndIDEVI 318
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE--REKAK 710

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 5454140   319 iptaplyKQILNLyaeENAIEDTifylgEALRRGVIDLDVFLK 361
Cdd:PRK03918 711 -------KELEKL---EKALERV-----EELREKVKKYKALLK 738
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 230-342 3.57e-04

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: 42.70  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140    230 LISAVSDKLRWRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMEnqS 309
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK--K 624

                          90       100       110
                  ....*....|....*....|....*....|...
gi 5454140    310 ENNDIDEvIIPTAPLYKQILNLYAEenAIEDTI 342
Cdd:TIGR04523 625 ENEKLSS-IIKNIKSKKNKLKQEVK--QIKETI 654
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 231-342 3.72e-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: 41.45  E-value: 3.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  231 ISAVSDKLRwRMKEEMDRAQA--ELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALE--KME 306
Cdd:COG1579  68 IEEVEARIK-KYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEekKAE 146

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5454140  307 NQSENNDIDeviiptaplyKQILNLYAEENAIEDTI 342
Cdd:COG1579 147 LDEELAELE----------AELEELEAEREELAAKI 172
PRK12704 PRK12704
phosphodiesterase; Provisional
 243-311 4.00e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 4.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5454140   243 KEEMDRAQAELnalkrtEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 311
Cdd:PRK12704  63 KEEIHKLRNEF------EKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 224-369 4.37e-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: 42.36  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140     224 DTIRASLiSAVSDKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALE 303
Cdd:TIGR02169  794 PEIQAEL-SKLEEEVS-RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5454140     304 KMENQsenndIDEVIIPTAPLYKQILNLYAEENAIEDtifylgealRRGVIDLDVFLKHVRLLSRK 369
Cdd:TIGR02169  872 ELEAA-----LRDLESRLGDLKKERDELEAQLRELER---------KIEELEAQIEKKRKRLSELK 923
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 243-313 5.20e-04

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: 39.96  E-value: 5.20e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5454140  243 KEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENND 313
Cdd:cd00179  12 RGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSSV 82
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 229-305 6.22e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 6.22e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5454140  229 SLISAVSDKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKM 305
Cdd:COG3883  16 PQIQAKQKELS-ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
PRK10698 PRK10698
phage shock protein PspA; Provisional
 223-302 7.60e-04

phage shock protein PspA; Provisional


Pssm-ID: 182657 [Multi-domain]  Cd Length: 222  Bit Score: 40.53  E-value: 7.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140   223 EDT---IRASLISAVSDKLRWRMKEEMDRAQ-------AELnALKRTEEDLKKG----HQKLEEMVTRLDQEVAEVDKNI 288
Cdd:PRK10698  37 EDTlveVRSTSARALAEKKQLTRRIEQAEAQqvewqekAEL-ALRKEKEDLARAalieKQKLTDLIATLEHEVTLVDETL 115

                         90
                 ....*....|....
gi 5454140   289 ELLKKKDEELSSAL 302
Cdd:PRK10698 116 ARMKKEIGELENKL 129
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
241-351 8.15e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140   241 RMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEViip 320
Cdd:COG4913  675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL--- 751

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 5454140   321 tAPLYKQIL----------NLYAEENAIEDTIFYLGEALRR 351
Cdd:COG4913  752 -EERFAAALgdaverelreNLEERIDALRARLNRAEEELER 791
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 227-310 9.00e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 9.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  227 RASLISAVSDKLRwRMKEEMDRAQAELNALKR----TEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSAL 302
Cdd:COG3883 120 RLSALSKIADADA-DLLEELKADKAELEAKKAeleaKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198


                ....*...
gi 5454140  303 EKMENQSE 310
Cdd:COG3883 199 AELEAELA 206
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 245-311 1.30e-03

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: 39.91  E-value: 1.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5454140  245 EMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 311
Cdd:COG1579  18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
231-378 1.44e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  231 ISAVSDKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQK--------------LEEMVTRLDQEVAEVDKNIELLKKkdE 296
Cdd:COG4372 103 LESLQEEAE-ELQEELEELQKERQDLEQQRKQLEAQIAElqseiaereeelkeLEEQLESLQEELAALEQELQALSE--A 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  297 ELSSALEKMENQSENNdidEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRAL 376
Cdd:COG4372 180 EAEQALDELLKEANRN---AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256


                ..
gi 5454140  377 MQ 378
Cdd:COG4372 257 LK 258
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-306 1.89e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5454140   236 DKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 306
Cdd:PRK03918 224 EKLE-KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 232-300 1.90e-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: 38.00  E-value: 1.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5454140    232 SAVSDKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEmvtRLDQEVAEVDKNIELLKKKDEELSS 300
Cdd:pfam07926  53 AEDIKALQ-ALREELNELKAEIAELKAEAESAKAELEESEE---SWEEQKKELEKELSELEKRIEDLNE 117
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
241-389 2.12e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  241 RMKEEMDRAQAELNALKR-----TEEDLKKGHQKLEEMVtrldQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDID 315
Cdd:COG4717 167 ELEAELAELQEELEELLEqlslaTEEELQDLAEELEELQ----QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5454140  316 EVIIPTAPLYKQ---ILNLYAEENAIEDTIFYLGEALrrgVIDLDVFLKHVRLLSRKQFQLRALMQKARKTAGLSDL 389
Cdd:COG4717 243 ERLKEARLLLLIaaaLLALLGLGGSLLSLILTIAGVL---FLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
243-351 2.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  243 KEEMDRAQAELNALKRTEEDLKKGHQKLEEMV---------TRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN-- 311
Cdd:COG4717  94 QEELEELEEELEELEAELEELREELEKLEKLLqllplyqelEALEAELAELPERLEELEERLEELRELEEELEELEAEla 173

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 5454140  312 ---NDIDEVIIPTAPLYKQILNLYAEE-NAIEDTIFYLGEALRR 351
Cdd:COG4717 174 elqEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEE 217
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 236-342 3.09e-03

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: 38.75  E-value: 3.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  236 DKLRWRMKE---EMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIellKKKDEELSS--------ALEK 304
Cdd:COG1579  20 DRLEHRLKElpaELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---KKYEEQLGNvrnnkeyeALQK 96

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 5454140  305 -MENQSENNDIDEviiptaplyKQILNLYAEENAIEDTI 342
Cdd:COG1579  97 eIESLKRRISDLE---------DEILELMERIEELEEEL 126
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 236-319 4.06e-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: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140    236 DKLRWRMKEEMDRAQAELNALKRTEEDLKKG-------HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSalEKMENQ 308
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES--EKKEKE 537

                          90
                  ....*....|.
gi 5454140    309 SENNDIDEVII 319
Cdd:TIGR04523 538 SKISDLEDELN 548
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 243-342 4.59e-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: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140    243 KEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN--NDIDEV--- 317
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNiqKNIDKIknk 195

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 5454140    318 ---------IIPT-----APLYKQILNLYAEENAIEDTI 342
Cdd:TIGR04523 196 llklelllsNLKKkiqknKSLESQISELKKQNNQLKDNI 234
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 225-293 5.15e-03

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 38.68  E-value: 5.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5454140    225 TIRASLisavsDKLRWRMKEEMdRAQAEL--NALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKK 293
Cdd:pfam03148 222 QLRELI-----DSILEQTANDL-RAQADAvnFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEK 286
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
227-368 6.12e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 6.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  227 RASLISAVSDKLRWR-MKEEMDRAQAELNALKRTEEDLKKGHQK--LEEMVTRLDQEVAEVDKNIELLKKKDEELSSALE 303
Cdd:COG4717 384 EEELRAALEQAEEYQeLKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELE 463

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5454140  304 KMEnqsENNDIDEviiptapLYKQI------LNLYAEENAIEDTIFYLGEALRRGVID--LDVFLKHV-RLLSR 368
Cdd:COG4717 464 QLE---EDGELAE-------LLQELeelkaeLRELAEEWAALKLALELLEEAREEYREerLPPVLERAsEYFSR 527
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
227-382 6.22e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140   227 RASLISAVSDkLRWRMKEeMDRAQAELNALKRTEEDLKKGHQKLEEmvtrLDQEVAEVDKNIELLKKKDEELSSALEKME 306
Cdd:COG4913  646 RREALQRLAE-YSWDEID-VASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLE 719

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140   307 NQSENndideviiptapLYKQILNLYAEENAIEDTI----FYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARK 382
Cdd:COG4913  720 KELEQ------------AEEELDELQDRLEAAEDLArlelRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-293 6.79e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 6.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 5454140   236 DKLRWRMK-EEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKK 293
Cdd:PRK03918 375 ERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 232-311 7.39e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 36.02  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140    232 SAVSDKLRWRMKEEMDRA-QAELNALKRTEEDLKKGH---QKLEEMVTRLDQEVAEVDKNIELLKKKD---EELSSALEK 304
Cdd:pfam18595   3 TLAEEKEELAELERKARElQAKIDALQVVEKDLRSCIkllEEIEAELAKLEEAKKKLKELRDALEEKEielRELERREER 82


                  ....*..
gi 5454140    305 MENQSEN 311
Cdd:pfam18595  83 LQRQLEN 89
RPN7 COG5187
26S proteasome regulatory complex component, contains PCI domain [Posttranslational ...
 264-365 8.79e-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: 8.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454140  264 KKGHQKLEEMVTRLDQEVAEvdkniELLKKKDE---ELSSALEKMENQSENNDIDEVIIPTAPLYKQILNLyaeENAIEd 340
Cdd:COG5187  66 EKGNPKTSASVIKFDRGRMN-----TLLKKNEEkieELDERIREKEEDNGETEGSEADRNIAEYYCQIMDI---QNGFE- 136

                        90       100
                ....*....|....*....|....*...
gi 5454140  341 tifYLGEALRRGV---IDLDVFLKHVRL 365
Cdd:COG5187 137 ---WMRRLMRDAMstgLKIDVFLCKIRL 161
 
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