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Conserved domains on  [gi|58037405|ref|NP_083508|]
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transmembrane and coiled-coil domain-containing protein 5B [Mus musculus]

Protein Classification

TMCO5 domain-containing protein( domain architecture ID 12171749)

TMCO5 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TMCO5 pfam14992
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ...
 28-306 1.14e-141

TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.


:

Pssm-ID: 464427 [Multi-domain]  Cd Length: 278  Bit Score: 400.63  E-value: 1.14e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405    28 LKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIAL--SIGRVPERDDFNEILAQKETALKDLELESAKLEKKN 105
Cdd:pfam14992   1 LNSLNSDLEKDLQRLDEANQVLLLKIQEKEEEIQSLEREITLtrSLAEDEEREELNFTIMEKEDALQELELETAKLEKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   106 KTLSKNVMELQKKISKGL-KNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHYIKKYQE 184
Cdd:pfam14992  81 EILVKSVMELQRKLSRKSdKNTGLEQETLKQMLEELKVKLQQSEESCADQEKELAKVESDYQSVHQLCEDQALCIKKYQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   185 ILREMEKEKEVMLLEKEISKAQNDSSQVVKpgstLVETIQSNMEKNIIKKQKRKFWLRHFRYLFFMVMIVIRLLGYVFFH 264
Cdd:pfam14992 161 ILRKMEEEKETRLLEKEVSKAQSNSSQRVK----LVETIQQNMEKTIIKKQKRIFWKRHFRYLFFMVLIFIRLLGYVLFH 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 58037405   265 LQYVNPDFLVDTLPMLMSRSSLKWLRDILFPFLTLEVEDVLP 306
Cdd:pfam14992 237 LQYINPDLLVDTLPKMLSRRTLWRLRCFLFPFLTLEVEDLLP 278
 
Name Accession Description Interval E-value
TMCO5 pfam14992
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ...
 28-306 1.14e-141

TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.


Pssm-ID: 464427 [Multi-domain]  Cd Length: 278  Bit Score: 400.63  E-value: 1.14e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405    28 LKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIAL--SIGRVPERDDFNEILAQKETALKDLELESAKLEKKN 105
Cdd:pfam14992   1 LNSLNSDLEKDLQRLDEANQVLLLKIQEKEEEIQSLEREITLtrSLAEDEEREELNFTIMEKEDALQELELETAKLEKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   106 KTLSKNVMELQKKISKGL-KNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHYIKKYQE 184
Cdd:pfam14992  81 EILVKSVMELQRKLSRKSdKNTGLEQETLKQMLEELKVKLQQSEESCADQEKELAKVESDYQSVHQLCEDQALCIKKYQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   185 ILREMEKEKEVMLLEKEISKAQNDSSQVVKpgstLVETIQSNMEKNIIKKQKRKFWLRHFRYLFFMVMIVIRLLGYVFFH 264
Cdd:pfam14992 161 ILRKMEEEKETRLLEKEVSKAQSNSSQRVK----LVETIQQNMEKTIIKKQKRIFWKRHFRYLFFMVLIFIRLLGYVLFH 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 58037405   265 LQYVNPDFLVDTLPMLMSRSSLKWLRDILFPFLTLEVEDVLP 306
Cdd:pfam14992 237 LQYINPDLLVDTLPKMLSRRTLWRLRCFLFPFLTLEVEDLLP 278
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-248 2.14e-07

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: 52.38  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405     16 TEIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIGRVPErddFNEILAQKETALKDLE 95
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLE 881

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405     96 LESAKLEKKNKTLSKNVMELQKKISKglknIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQ 175
Cdd:TIGR02169  882 SRLGDLKKERDELEAQLRELERKIEE----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ 957

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405    176 ahyiKKYQEILREMEKEKEV-MLLEKEISKAQNDSSQVVKPGSTLVETIQSNMEK-NIIKKQKRKFWL-------RHFRY 246
Cdd:TIGR02169  958 ----AELQRVEEEIRALEPVnMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERiEEYEKKKREVFMeafeainENFNE 1033


                   ..
gi 58037405    247 LF 248
Cdd:TIGR02169 1034 IF 1035
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-238 6.19e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   21 LEAIKQNLKYLNSDLEKDLQRLDEANQIL----------LRKIQKKEESIQSLERDIALSIGRVPERDDFNEILAQKETA 90
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIkekekeleevLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   91 LKDLELESAKLEKKNKTLSKNVMELQKKISKgLKNIASDPETLKKKVTEFkVKLQKSTESCAQQEKEIAKMESDYQSVFQ 170
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEEIN 324

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58037405  171 LCEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQSNMEKNIIKKQKRK 238
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 19-225 3.85e-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: 3.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  19 PTLEAIKQNLKYLNSD---LEKDLQRLDEANQILLRKIQKKEESIQSLERDIalsigrvperDDFNEILAQKETALKDLE 95
Cdd:COG3883  16 PQIQAKQKELSELQAEleaAQAELDALQAELEELNEEYNELQAELEALQAEI----------DKLQAEIAEAEAEIEERR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  96 lesAKLEKKNKTL---------------SKNV------MELQKKISKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQ 154
Cdd:COG3883  86 ---EELGERARALyrsggsvsyldvllgSESFsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037405 155 EKEIAKMESDYQSVFqlcEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQS 225
Cdd:COG3883 163 KAELEAAKAELEAQQ---AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
 
Name Accession Description Interval E-value
TMCO5 pfam14992
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ...
 28-306 1.14e-141

TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.


Pssm-ID: 464427 [Multi-domain]  Cd Length: 278  Bit Score: 400.63  E-value: 1.14e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405    28 LKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIAL--SIGRVPERDDFNEILAQKETALKDLELESAKLEKKN 105
Cdd:pfam14992   1 LNSLNSDLEKDLQRLDEANQVLLLKIQEKEEEIQSLEREITLtrSLAEDEEREELNFTIMEKEDALQELELETAKLEKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   106 KTLSKNVMELQKKISKGL-KNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHYIKKYQE 184
Cdd:pfam14992  81 EILVKSVMELQRKLSRKSdKNTGLEQETLKQMLEELKVKLQQSEESCADQEKELAKVESDYQSVHQLCEDQALCIKKYQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   185 ILREMEKEKEVMLLEKEISKAQNDSSQVVKpgstLVETIQSNMEKNIIKKQKRKFWLRHFRYLFFMVMIVIRLLGYVFFH 264
Cdd:pfam14992 161 ILRKMEEEKETRLLEKEVSKAQSNSSQRVK----LVETIQQNMEKTIIKKQKRIFWKRHFRYLFFMVLIFIRLLGYVLFH 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 58037405   265 LQYVNPDFLVDTLPMLMSRSSLKWLRDILFPFLTLEVEDVLP 306
Cdd:pfam14992 237 LQYINPDLLVDTLPKMLSRRTLWRLRCFLFPFLTLEVEDLLP 278
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-248 2.14e-07

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: 52.38  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405     16 TEIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIGRVPErddFNEILAQKETALKDLE 95
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLE 881

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405     96 LESAKLEKKNKTLSKNVMELQKKISKglknIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQ 175
Cdd:TIGR02169  882 SRLGDLKKERDELEAQLRELERKIEE----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ 957

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405    176 ahyiKKYQEILREMEKEKEV-MLLEKEISKAQNDSSQVVKPGSTLVETIQSNMEK-NIIKKQKRKFWL-------RHFRY 246
Cdd:TIGR02169  958 ----AELQRVEEEIRALEPVnMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERiEEYEKKKREVFMeafeainENFNE 1033


                   ..
gi 58037405    247 LF 248
Cdd:TIGR02169 1034 IF 1035
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-238 6.19e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   21 LEAIKQNLKYLNSDLEKDLQRLDEANQIL----------LRKIQKKEESIQSLERDIALSIGRVPERDDFNEILAQKETA 90
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIkekekeleevLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   91 LKDLELESAKLEKKNKTLSKNVMELQKKISKgLKNIASDPETLKKKVTEFkVKLQKSTESCAQQEKEIAKMESDYQSVFQ 170
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEEIN 324

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58037405  171 LCEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQSNMEKNIIKKQKRK 238
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 33-214 1.47e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 45.96  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405    33 SDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIAlsigrvpERDDFNEILAQKETALKDlelesaklEKKNKTLSKNV 112
Cdd:pfam15905  97 QALEEELEKVEAKLNAAVREKTSLSASVASLEKQLL-------ELTRVNELLKAKFSEDGT--------QKKMSSLSMEL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   113 MELQKKISKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHYIKKYQEILREMEKE 192
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKY 241

                         170       180
                  ....*....|....*....|..
gi 58037405   193 KEVMLLEKEISKAQNDSSQVVK 214
Cdd:pfam15905 242 KLDIAQLEELLKEKNDEIESLK 263
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-223 2.13e-05

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: 46.21  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405     16 TEIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIGRvpeRDDFNEILAQKETALKDLE 95
Cdd:TIGR02169  294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR---RDKLTEEYAELKEELEDLR 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405     96 LESAKLEKKNKTLSKNVMELQKKISKG-------LKNIASDPETLKKKVTE-------FKVKLQKSTESCAQQEKEIAKM 161
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYREKLEKLkreinelKRELDRLQEELQRLSEEladlnaaIAGIEAKINELEEEKEDKALEI 450

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58037405    162 ESDYQSVFQLCEDQAHYIKKY---QEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETI 223
Cdd:TIGR02169  451 KKQEWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 19-225 3.85e-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: 3.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  19 PTLEAIKQNLKYLNSD---LEKDLQRLDEANQILLRKIQKKEESIQSLERDIalsigrvperDDFNEILAQKETALKDLE 95
Cdd:COG3883  16 PQIQAKQKELSELQAEleaAQAELDALQAELEELNEEYNELQAELEALQAEI----------DKLQAEIAEAEAEIEERR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  96 lesAKLEKKNKTL---------------SKNV------MELQKKISKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQ 154
Cdd:COG3883  86 ---EELGERARALyrsggsvsyldvllgSESFsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037405 155 EKEIAKMESDYQSVFqlcEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQS 225
Cdd:COG3883 163 KAELEAAKAELEAQQ---AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
 58-199 4.90e-04

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 41.36  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405    58 ESIQSLERDIALsigrvperddfNEILAQKETALKDLELESAKLEKKNKTLSKNVMELQKKISK--GLKNIASDpetLKK 135
Cdd:pfam15066 305 ESLQPLEEDMAL-----------NEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKqqVFVDIINK---LKE 370

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58037405   136 KVTE-----FKVKLQKStescaqqekEIAKMESDYQSVfqLCEDQAHyikkyqeiLREMEKEKEVMLLE 199
Cdd:pfam15066 371 NVEEliedkYNVILEKN---------DINKTLQNLQEI--LANTQKH--------LQESRKEKETLQLE 420
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-211 6.63e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 6.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  10 DDEAEITEIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIgrvPERDDFNEILAQKET 89
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEE 365

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  90 ALKDLELESAKLEKKNKTLSKNVMELQKKISKGLKNIASDPETLKKKVTEfKVKLQKSTESCAQQEKEIAKMESDYQSVF 169
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEAL 444

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 58037405 170 Q--LCEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQ 211
Cdd:COG1196 445 EeaAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1-127 1.03e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   1 MEDAGQNPLDDEAEITEIPTLEAIKQNLKYLnSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSigRVPERDDf 80
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEI-RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA--RSEERRE- 460

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 58037405  81 neilAQKETALKDLELESAKLEKKNKTLSKNVMELQKKISKgLKNIA 127
Cdd:COG2433 461 ----IRKDREISRLDREIERLERELEEERERIEELKRKLER-LKELW 502
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 38-201 1.08e-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: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  38 DLQRLDEANQILLRKIQKKEESIQSLERDIAlsigrvperdDFNEILAQKETALKDLELESAKLEKKNKTLSKNVMELQK 117
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPAELAELEDELA----------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405 118 KI-----SKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQsvfQLCEDQAHYIKKYQEILREMEKE 192
Cdd:COG1579  81 QLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAE 157


                ....*....
gi 58037405 193 KEVMLLEKE 201
Cdd:COG1579 158 LEELEAERE 166
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 26-238 3.30e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405    26 QNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDI----ALSIGRVPERDDFNEILAQKETALKDLELESAKL 101
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIerlkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   102 EKKNKTLS---KNVMELQKKISKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHY 178
Cdd:TIGR04523 467 ETQLKVLSrsiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58037405   179 IKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQ--SNMEKNIIKKQKRK 238
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDqkEKEKKDLIKEIEEK 608
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 21-131 4.73e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 4.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  21 LEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERdialsigrvpERDDFNEILAQKETALKDLELESAK 100
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE----------ERAALEALKAERQKLLARLEKELAE 210

                        90       100       110
                ....*....|....*....|....*....|.
gi 58037405 101 LEKKNKTLSKNVMELQKKISKGLKNIASDPE 131
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAAAAE 241
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 17-214 6.28e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.82  E-value: 6.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  17 EIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIGrvpERDDFNEILAQKETALKDLEL 96
Cdd:COG4942  35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---EIAELRAELEAQKEELAELLR 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405  97 ESAKLEKKNKTL----------SKNVMELQKKISKGLKN----IASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKME 162
Cdd:COG4942 112 ALYRLGRQPPLAlllspedfldAVRRLQYLKYLAPARREqaeeLRADLAELAALRAELEAERAELEALLAELEEERAALE 191

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 58037405 163 SDYQSVFQLCEDQAHYIKKYQEILREMEKEKEvmLLEKEISKAQNDSSQVVK 214
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAE--ELEALIARLEAEAAAAAE 241
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 35-235 8.49e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 37.80  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405    35 LEKDLQRLDEANQILLRKIQKKEES-----IQSLERDIALSIGRVP----ERDDFNEILAQKETALKDLELESAKLEKKN 105
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQEEarqreVRRLEEERAREMERVRleeqERQQQVERLRQQEEERKRKKLELEKEKRDR 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037405   106 KTLSK-NVMELQKKISKGLKNIASdpETLKKKVTEFKVKlQKSTESCAQQEKEIAKMESDYQSVFQ---LCEDQAHYIKK 181
Cdd:pfam17380 487 KRAEEqRRKILEKELEERKQAMIE--EERKRKLLEKEME-ERQKAIYEEERRREAEEERRKQQEMEerrRIQEQMRKATE 563

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 58037405   182 YQEILREMEKEKEVMLLEKEISKAQNDSsqvvkPGSTLVETIQSNMEKNIIKKQ 235
Cdd:pfam17380 564 ERSRLEAMEREREMMRQIVESEKARAEY-----EATTPITTIKPIYRPRISEYQ 612
 
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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