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Conserved domains on  [gi|530395744|ref|XP_005253165|]
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tumor susceptibility gene 101 protein isoform X1 [Homo sapiens]

Protein Classification

UEV_TSG101-like and Vps23_core domain-containing protein( domain architecture ID 10530305)

protein containing domains UEV_TSG101-like, Atg16_CCD, and Vps23_core

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) ...
 1-87 2.39e-52

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: 168.59  E-value: 2.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744    1 MNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMI 80
Cdd:pfam05743  33 LNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVNHHVDAQGRVYLPYLHNWNHPSSNLVDLVQELA 112


                  ....*..
gi 530395744   81 VVFGDEP 87
Cdd:pfam05743 113 QVFQEDP 119
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 264-323 4.17e-29

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: 106.39  E-value: 4.17e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  264 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 323
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-297 5.84e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 5.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 159 TTVGPSRDGTISEDTIRASLISAVSDKLRwRMKEEMDRAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQ 227
Cdd:COG4372    6 EKVGKARLSLFGLRPKTGILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEE 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 228 EVAEVDKNIELLKKKDEELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 297
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) ...
 1-87 2.39e-52

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: 168.59  E-value: 2.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744    1 MNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMI 80
Cdd:pfam05743  33 LNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVNHHVDAQGRVYLPYLHNWNHPSSNLVDLVQELA 112


                  ....*..
gi 530395744   81 VVFGDEP 87
Cdd:pfam05743 113 QVFQEDP 119
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 1-91 7.29e-50

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: 162.48  E-value: 7.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744   1 MNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTI-KTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVM 79
Cdd:cd11685   35 LCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMIiKPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQEL 114

                         90
                 ....*....|..
gi 530395744  80 IVVFGDEPPVFS 91
Cdd:cd11685  115 SAVFSEEPPVYS 126
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 264-323 4.17e-29

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: 106.39  E-value: 4.17e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  264 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 323
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 1-103 2.54e-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: 2.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744     1 MNLTGTIPVPYRGNTYniPICLWLLDTYPYNPPICFVKPTssmtiKTGKHVDANGKIYLPYLHE--WKhPQSDLLGLIQV 78
Cdd:smart00212  32 GTIVGPPGTPYEGGVF--KLTIEFPEDYPFKPPKVKFITK-----IYHPNVDSSGEICLDILKQekWS-PALTLETVLLS 103

                           90       100
                   ....*....|....*....|....*
gi 530395744    79 mIVVFGDEPPVFSRPISASYPPYQA 103
Cdd:smart00212 104 -LQSLLSEPNPDSPLNADAAELYKK 127
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-297 5.84e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 5.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 159 TTVGPSRDGTISEDTIRASLISAVSDKLRwRMKEEMDRAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQ 227
Cdd:COG4372    6 EKVGKARLSLFGLRPKTGILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEE 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 228 EVAEVDKNIELLKKKDEELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 297
Cdd:COG4372   85 LNEQLQAAQAELAQAQEELESLQEEAEELQE--ELEELQ-------KERQDLEQQRKQLEAQIAELQSEI 145
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 184-240 3.69e-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: 46.74  E-value: 3.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395744  184 DKLRWRMKEEMDRAQAE----LNALK-RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLK 240
Cdd:pfam07798  89 EKLKQRLREEITKLKADvrldLNLEKgRIREELKAQELKIQETNNKIDTEIANLRTQIESVK 150
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 186-331 1.06e-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: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744   186 LRW-RMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSE------ 258
Cdd:TIGR02168  232 LRLeELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerl 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744   259 ---NNDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYL-----------------GEALRRGVIDLDvflKHVRLLSRKQ 318
Cdd:TIGR02168  312 anlERQLEELEAQLEELESKLDELAEELAELEEKLEELkeelesleaeleeleaeLEELESRLEELE---EQLETLRSKV 388

                          170
                   ....*....|...
gi 530395744   319 FQLRALMQKARKT 331
Cdd:TIGR02168  389 AQLELQIASLNNE 401
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 198-261 2.85e-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: 42.17  E-value: 2.85e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395744 198 QAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLkkKDE------ELSSALEKMEN-QSENND 261
Cdd:cd22887    3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL--NDElialqiENNLLEEKLRKlQEENDE 71
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
192-309 9.17e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 9.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 192 EEMDRAQAELNALKRTEEDLKKG-----HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENndIDEVI 266
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE--REKAK 710

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530395744 267 iptaplyKQILNLyaeENAIEDTifylgEALRRGVIDLDVFLK 309
Cdd:PRK03918 711 -------KELEKL---EKALERV-----EELREKVKKYKALLK 738
 
Name Accession Description Interval E-value
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 1-87 2.39e-52

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: 168.59  E-value: 2.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744    1 MNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMI 80
Cdd:pfam05743  33 LNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVNHHVDAQGRVYLPYLHNWNHPSSNLVDLVQELA 112


                  ....*..
gi 530395744   81 VVFGDEP 87
Cdd:pfam05743 113 QVFQEDP 119
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 1-91 7.29e-50

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: 162.48  E-value: 7.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744   1 MNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTI-KTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVM 79
Cdd:cd11685   35 LCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMIiKPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQEL 114

                         90
                 ....*....|..
gi 530395744  80 IVVFGDEPPVFS 91
Cdd:cd11685  115 SAVFSEEPPVYS 126
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 264-323 4.17e-29

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: 106.39  E-value: 4.17e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  264 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 323
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 1-103 2.54e-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: 2.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744     1 MNLTGTIPVPYRGNTYniPICLWLLDTYPYNPPICFVKPTssmtiKTGKHVDANGKIYLPYLHE--WKhPQSDLLGLIQV 78
Cdd:smart00212  32 GTIVGPPGTPYEGGVF--KLTIEFPEDYPFKPPKVKFITK-----IYHPNVDSSGEICLDILKQekWS-PALTLETVLLS 103

                           90       100
                   ....*....|....*....|....*
gi 530395744    79 mIVVFGDEPPVFSRPISASYPPYQA 103
Cdd:smart00212 104 -LQSLLSEPNPDSPLNADAAELYKK 127
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-297 5.84e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 5.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 159 TTVGPSRDGTISEDTIRASLISAVSDKLRwRMKEEMDRAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQ 227
Cdd:COG4372    6 EKVGKARLSLFGLRPKTGILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEE 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 228 EVAEVDKNIELLKKKDEELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 297
Cdd:COG4372   85 LNEQLQAAQAELAQAQEELESLQEEAEELQE--ELEELQ-------KERQDLEQQRKQLEAQIAELQSEI 145
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
189-317 6.08e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 6.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 189 RMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIP 268
Cdd:COG4372   98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530395744 269 TAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRK 317
Cdd:COG4372  178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 184-240 3.69e-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: 46.74  E-value: 3.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395744  184 DKLRWRMKEEMDRAQAE----LNALK-RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLK 240
Cdd:pfam07798  89 EKLKQRLREEITKLKADvrldLNLEKgRIREELKAQELKIQETNNKIDTEIANLRTQIESVK 150
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 186-331 1.06e-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: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744   186 LRW-RMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSE------ 258
Cdd:TIGR02168  232 LRLeELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerl 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744   259 ---NNDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYL-----------------GEALRRGVIDLDvflKHVRLLSRKQ 318
Cdd:TIGR02168  312 anlERQLEELEAQLEELESKLDELAEELAELEEKLEELkeelesleaeleeleaeLEELESRLEELE---EQLETLRSKV 388

                          170
                   ....*....|...
gi 530395744   319 FQLRALMQKARKT 331
Cdd:TIGR02168  389 AQLELQIASLNNE 401
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 184-252 1.38e-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: 45.69  E-value: 1.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530395744 184 DKLRWRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEK 252
Cdd:COG1579  106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 198-261 2.85e-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: 42.17  E-value: 2.85e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395744 198 QAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLkkKDE------ELSSALEKMEN-QSENND 261
Cdd:cd22887    3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL--NDElialqiENNLLEEKLRKlQEENDE 71
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 191-259 4.91e-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: 42.21  E-value: 4.91e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395744  191 KEEMDRAQAELNA-LKRTEEDLKKGHQKL---EEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 259
Cdd:pfam20492   1 REEAEREKQELEErLKQYEEETKKAQEELeesEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEM 73
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 191-330 5.07e-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: 5.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744   191 KEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKK----DEELSSALEKMENQSEN------- 259
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEieellkk 429

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395744   260 ---NDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARK 330
Cdd:TIGR02168  430 leeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 184-258 5.67e-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: 42.21  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  184 DKLRwRMKEEMDRAQAELNA-----------LKRTEED---LKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSA 249
Cdd:pfam20492  13 ERLK-QYEEETKKAQEELEEseetaeeleeeRRQAEEEaerLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE 91


                  ....*....
gi 530395744  250 LEKMENQSE 258
Cdd:pfam20492  92 IARLEEEVE 100
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
192-309 9.17e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 9.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 192 EEMDRAQAELNALKRTEEDLKKG-----HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENndIDEVI 266
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE--REKAK 710

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530395744 267 iptaplyKQILNLyaeENAIEDTifylgEALRRGVIDLDVFLK 309
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 ...
 178-290 1.15e-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: 43.86  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  178 LISAVSDKLRWRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMEnqS 257
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK--K 624

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530395744  258 ENNDIDEvIIPTAPLYKQILNLYAEenAIEDTI 290
Cdd:TIGR04523 625 ENEKLSS-IIKNIKSKKNKLKQEVK--QIKETI 654
PRK10325 PRK10325
heat shock protein GrpE; Provisional
 189-254 1.21e-04

heat shock protein GrpE; Provisional


Pssm-ID: 182379 [Multi-domain]  Cd Length: 197  Bit Score: 42.35  E-value: 1.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530395744 189 RMKEEMDRAQAELNALKR-TEEDLKKGHQ-KLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 254
Cdd:PRK10325  57 RERDGILRVKAEMENLRRrTELDIEKAHKfALEKFINELLPVIDSLDRALEVADKANPDMSAMVEGIE 124
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 172-317 2.13e-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: 43.13  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744   172 DTIRASLiSAVSDKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALE 251
Cdd:TIGR02169  794 PEIQAEL-SKLEEEVS-RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530395744   252 KMENQsenndIDEVIIPTAPLYKQILNLYAEENAIEDtifylgealRRGVIDLDVFLKHVRLLSRK 317
Cdd:TIGR02169  872 ELEAA-----LRDLESRLGDLKKERDELEAQLRELER---------KIEELEAQIEKKRKRLSELK 923
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 179-290 2.22e-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: 41.83  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 179 ISAVSDKLRwRMKEEMDRAQA--ELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALE--KME 254
Cdd:COG1579   68 IEEVEARIK-KYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEekKAE 146

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530395744 255 NQSENNDIDeviiptaplyKQILNLYAEENAIEDTI 290
Cdd:COG1579  147 LDEELAELE----------AELEELEAEREELAAKI 172
PRK12704 PRK12704
phosphodiesterase; Provisional
 191-259 3.01e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 3.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530395744 191 KEEMDRAQAELnalkrtEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 259
Cdd:PRK12704  63 KEEIHKLRNEF------EKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 191-261 3.41e-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: 40.35  E-value: 3.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395744 191 KEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENND 261
Cdd:cd00179   12 RGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSSV 82
PRK10698 PRK10698
phage shock protein PspA; Provisional
 171-250 4.48e-04

phage shock protein PspA; Provisional


Pssm-ID: 182657 [Multi-domain]  Cd Length: 222  Bit Score: 40.91  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 171 EDT---IRASLISAVSDKLRWRMKEEMDRAQ-------AELnALKRTEEDLKKG----HQKLEEMVTRLDQEVAEVDKNI 236
Cdd:PRK10698  37 EDTlveVRSTSARALAEKKQLTRRIEQAEAQqvewqekAEL-ALRKEKEDLARAalieKQKLTDLIATLEHEVTLVDETL 115

                         90
                 ....*....|....
gi 530395744 237 ELLKKKDEELSSAL 250
Cdd:PRK10698 116 ARMKKEIGELENKL 129
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 177-253 4.91e-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: 4.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530395744 177 SLISAVSDKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKM 253
Cdd:COG3883   16 PQIQAKQKELS-ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
189-299 6.33e-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: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  189 RMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEViip 268
Cdd:COG4913   675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL--- 751

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 530395744  269 tAPLYKQIL----------NLYAEENAIEDTIFYLGEALRR 299
Cdd:COG4913   752 -EERFAAALgdaverelreNLEERIDALRARLNRAEEELER 791
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
179-326 6.34e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 179 ISAVSDKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQK--------------LEEMVTRLDQEVAEVDKNIELLKKkdE 244
Cdd:COG4372  103 LESLQEEAE-ELQEELEELQKERQDLEQQRKQLEAQIAElqseiaereeelkeLEEQLESLQEELAALEQELQALSE--A 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 245 ELSSALEKMENQSENNdidEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRAL 324
Cdd:COG4372  180 EAEQALDELLKEANRN---AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256


                 ..
gi 530395744 325 MQ 326
Cdd:COG4372  257 LK 258
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 175-258 7.13e-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: 7.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 175 RASLISAVSDKLRwRMKEEMDRAQAELNALKR----TEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSAL 250
Cdd:COG3883  120 RLSALSKIADADA-DLLEELKADKAELEAKKAeleaKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198


                 ....*...
gi 530395744 251 EKMENQSE 258
Cdd:COG3883  199 AELEAELA 206
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 193-259 8.71e-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: 40.29  E-value: 8.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530395744 193 EMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 259
Cdd:COG1579   18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
184-254 9.47e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 9.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395744 184 DKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 254
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 ...
 180-248 1.37e-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: 38.39  E-value: 1.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530395744  180 SAVSDKLRwRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEmvtRLDQEVAEVDKNIELLKKKDEELSS 248
Cdd:pfam07926  53 AEDIKALQ-ALREELNELKAEIAELKAEAESAKAELEESEE---SWEEQKKELEKELSELEKRIEDLNE 117
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 191-290 1.42e-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: 40.39  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  191 KEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN--NDIDEV--- 265
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNiqKNIDKIknk 195

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530395744  266 ---------IIPT-----APLYKQILNLYAEENAIEDTI 290
Cdd:TIGR04523 196 llklelllsNLKKkiqknKSLESQISELKKQNNQLKDNI 234
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 184-267 1.47e-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: 40.39  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  184 DKLRWRMKEEMDRAQAELNALKRTEEDLKKG-------HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSalEKMENQ 256
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES--EKKEKE 537

                          90
                  ....*....|.
gi 530395744  257 SENNDIDEVII 267
Cdd:TIGR04523 538 SKISDLEDELN 548
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
189-337 1.67e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 189 RMKEEMDRAQAELNALKR-----TEEDLKKGHQKLEEMVtrldQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDID 263
Cdd:COG4717  167 ELEAELAELQEELEELLEqlslaTEEELQDLAEELEELQ----QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530395744 264 EVIIPTAPLYKQ---ILNLYAEENAIEDTIFYLGEALrrgVIDLDVFLKHVRLLSRKQFQLRALMQKARKTAGLSDL 337
Cdd:COG4717  243 ERLKEARLLLLIaaaLLALLGLGGSLLSLILTIAGVL---FLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 184-290 1.74e-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: 39.14  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 184 DKLRWRMKE---EMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIellKKKDEELSS--------ALEK 252
Cdd:COG1579   20 DRLEHRLKElpaELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---KKYEEQLGNvrnnkeyeALQK 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530395744 253 -MENQSENNDIDEviiptaplyKQILNLYAEENAIEDTI 290
Cdd:COG1579   97 eIESLKRRISDLE---------DEILELMERIEELEEEL 126
Caldesmon pfam02029
Caldesmon;
182-258 2.04e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.85  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  182 VSDKLRWRMKEEMDRAQAELNALKRTE---EDLKKGHQKLE-EMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQS 257
Cdd:pfam02029 221 VTTKRRQGGLSQSQEREEEAEVFLEAEqklEELRRRRQEKEsEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRR 300


                  .
gi 530395744  258 E 258
Cdd:pfam02029 301 K 301
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
191-299 2.19e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 191 KEEMDRAQAELNALKRTEEDLKKGHQKLEEMV---------TRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN-- 259
Cdd:COG4717   94 QEELEELEEELEELEAELEELREELEKLEKLLqllplyqelEALEAELAELPERLEELEERLEELRELEEELEELEAEla 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530395744 260 ---NDIDEVIIPTAPLYKQILNLYAEE-NAIEDTIFYLGEALRR 299
Cdd:COG4717  174 elqEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEE 217
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
184-241 3.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 3.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530395744 184 DKLRWRMK-EEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKK 241
Cdd:PRK03918 375 ERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
RPN7 COG5187
26S proteasome regulatory complex component, contains PCI domain [Posttranslational ...
 212-313 3.36e-03

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


Pssm-ID: 227514 [Multi-domain]  Cd Length: 412  Bit Score: 39.13  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 212 KKGHQKLEEMVTRLDQEVAEvdkniELLKKKDE---ELSSALEKMENQSENNDIDEVIIPTAPLYKQILNLyaeENAIEd 288
Cdd:COG5187   66 EKGNPKTSASVIKFDRGRMN-----TLLKKNEEkieELDERIREKEEDNGETEGSEADRNIAEYYCQIMDI---QNGFE- 136

                         90       100
                 ....*....|....*....|....*...
gi 530395744 289 tifYLGEALRRGV---IDLDVFLKHVRL 313
Cdd:COG5187  137 ---WMRRLMRDAMstgLKIDVFLCKIRL 161
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 173-241 3.97e-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: 3.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395744  173 TIRASLisavsDKLRWRMKEEMdRAQAEL--NALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKK 241
Cdd:pfam03148 222 QLRELI-----DSILEQTANDL-RAQADAvnFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEK 286
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
175-316 4.85e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744 175 RASLISAVSDKLRWR-MKEEMDRAQAELNALKRTEEDLKKGHQK--LEEMVTRLDQEVAEVDKNIELLKKKDEELSSALE 251
Cdd:COG4717  384 EEELRAALEQAEEYQeLKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELE 463

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395744 252 KMEnqsENNDIDEviiptapLYKQI------LNLYAEENAIEDTIFYLGEALRRGVID--LDVFLKHV-RLLSR 316
Cdd:COG4717  464 QLE---EDGELAE-------LLQELeelkaeLRELAEEWAALKLALELLEEAREEYREerLPPVLERAsEYFSR 527
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-330 4.91e-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: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  175 RASLISAVSDkLRWRMKEeMDRAQAELNALKRTEEDLKKGHQKLEEmvtrLDQEVAEVDKNIELLKKKDEELSSALEKME 254
Cdd:COG4913   646 RREALQRLAE-YSWDEID-VASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLE 719

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  255 NQSENndideviiptapLYKQILNLYAEENAIEDTI----FYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARK 330
Cdd:COG4913   720 KELEQ------------AEEELDELQDRLEAAEDLArlelRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 180-259 5.60e-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: 36.41  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395744  180 SAVSDKLRWRMKEEMDRA-QAELNALKRTEEDLKKGH---QKLEEMVTRLDQEVAEVDKNIELLKKKD---EELSSALEK 252
Cdd:pfam18595   3 TLAEEKEELAELERKARElQAKIDALQVVEKDLRSCIkllEEIEAELAKLEEAKKKLKELRDALEEKEielRELERREER 82


                  ....*..
gi 530395744  253 MENQSEN 259
Cdd:pfam18595  83 LQRQLEN 89
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 197-266 8.20e-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: 37.01  E-value: 8.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395744 197 AQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVA---EVDKNIELLKKKDEELSSALEKMEN--QSENNDIDEVI 266
Cdd:cd21116  114 VTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAvlnALKNQLNSLAEQIDAAIDALEKLSNdwQTLDSDIKELI 188
 
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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