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Conserved domains on  [gi|161082844|ref|NP_001097569|]
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nudE, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDE_C super family cl23541
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 129-208 1.18e-09

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


The actual alignment was detected with superfamily member pfam04880:

Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 56.72  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  129 SIENFEKMLDQAYEKNALLELEV----DEKGLLQEKLQRLMDETRDLKQELNVKSRFTPVVNGTSvPTANDTNTVNSSMN 204
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRS-PSTPSLQTLEIFDR 79


                  ....
gi 161082844  205 SSAS 208
Cdd:pfam04880  80 SPAV 83
GAS super family cl25894
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 73-167 1.53e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


The actual alignment was detected with superfamily member pfam13851:

Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 45.28  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   73 ENESLKLKLESHGIDMSNMEKQLETVKKDRDTMKVY---LRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLEL 149
Cdd:pfam13851  55 ENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLkarLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQ 134

                          90       100
                  ....*....|....*....|...
gi 161082844  150 EVDEKG-----LLQEKLQRLMDE 167
Cdd:pfam13851 135 DVQQKTglknlLLEKKLQALGET 157
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 129-208 1.18e-09

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 56.72  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  129 SIENFEKMLDQAYEKNALLELEV----DEKGLLQEKLQRLMDETRDLKQELNVKSRFTPVVNGTSvPTANDTNTVNSSMN 204
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRS-PSTPSLQTLEIFDR 79


                  ....
gi 161082844  205 SSAS 208
Cdd:pfam04880  80 SPAV 83
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 73-167 1.53e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 45.28  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   73 ENESLKLKLESHGIDMSNMEKQLETVKKDRDTMKVY---LRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLEL 149
Cdd:pfam13851  55 ENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLkarLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQ 134

                          90       100
                  ....*....|....*....|...
gi 161082844  150 EVDEKG-----LLQEKLQRLMDE 167
Cdd:pfam13851 135 DVQQKTglknlLLEKKLQALGET 157
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-175 3.93e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 3.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    11 EDECRYWKERSKQYHKEWTDVKQEYDEFVEQSREMEIEMDAT----------LDQKQSIIKDLTAKLTMFERENESLKLK 80
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATerrledleeqIEELSEDIESLAAEIEELEELIEELESE 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    81 LESHGIDMSNMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAyeknallelevdeKGLLQEK 160
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL-------------EVRIDNL 941

                          170
                   ....*....|....*
gi 161082844   161 LQRLMDETRDLKQEL 175
Cdd:TIGR02168  942 QERLSEEYSLTLEEA 956
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-180 9.40e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 9.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   12 DECRYWKERSKQYHKEwtdvkQEYDEFVEQSREMEIEMDATLDQkqsiIKDLTAKLTMFERENESLKLKLESH-GIDMSN 90
Cdd:COG4913   272 AELEYLRAALRLWFAQ-----RRLELLEAELEELRAELARLEAE----LERLEARLDALREELDELEAQIRGNgGDRLEQ 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   91 MEKQLETVKKDRDTMKvylRQLEQKNDDLERAHRILNESIENFEKMLDQAyekNALLELEVDEKGLLQEKLQRLMDETRD 170
Cdd:COG4913   343 LEREIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRD 416

                         170
                  ....*....|
gi 161082844  171 LKQELNVKSR 180
Cdd:COG4913   417 LRRELRELEA 426
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 30-241 2.78e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  30 DVKQEYDEFVEQSREMEIEMDAT---LDQKQSIIKDLTAKL-----TMFERENESLKLK--LESHGID------------ 87
Cdd:COG3883   48 ELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELgerarALYRSGGSVSYLDvlLGSESFSdfldrlsalski 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  88 MSNMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLELEVDEkglLQEKLQRLMDE 167
Cdd:COG3883  128 ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA---AEAQLAELEAE 204

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161082844 168 TRDLKQELNVKSRFTPVVNGTSVPTANDTNTVNSSMNSSASLPNGIVANGELVKHDNAVATRATSVSVNALNGS 241
Cdd:COG3883  205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
18-183 3.16e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  18 KERSKQYHKEWTDVKQEYDEFVEQSREMEIEMDATLDQKQSIiKDLTAKLTMFERENESLKLKLESHGIDMSNMEKQLET 97
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  98 VKKDRD--------------------TMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALL-ELEVDEKGL 156
Cdd:PRK03918 271 LKKEIEeleekvkelkelkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLeELKKKLKEL 350

                        170       180       190
                 ....*....|....*....|....*....|...
gi 161082844 157 LQ-----EKLQRLMDETRDLKQELN-VKSRFTP 183
Cdd:PRK03918 351 EKrleelEERHELYEEAKAKKEELErLKKRLTG 383
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 129-208 1.18e-09

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 56.72  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  129 SIENFEKMLDQAYEKNALLELEV----DEKGLLQEKLQRLMDETRDLKQELNVKSRFTPVVNGTSvPTANDTNTVNSSMN 204
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRS-PSTPSLQTLEIFDR 79


                  ....
gi 161082844  205 SSAS 208
Cdd:pfam04880  80 SPAV 83
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 73-167 1.53e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 45.28  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   73 ENESLKLKLESHGIDMSNMEKQLETVKKDRDTMKVY---LRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLEL 149
Cdd:pfam13851  55 ENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLkarLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQ 134

                          90       100
                  ....*....|....*....|...
gi 161082844  150 EVDEKG-----LLQEKLQRLMDE 167
Cdd:pfam13851 135 DVQQKTglknlLLEKKLQALGET 157
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-175 3.93e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 3.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    11 EDECRYWKERSKQYHKEWTDVKQEYDEFVEQSREMEIEMDAT----------LDQKQSIIKDLTAKLTMFERENESLKLK 80
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATerrledleeqIEELSEDIESLAAEIEELEELIEELESE 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    81 LESHGIDMSNMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAyeknallelevdeKGLLQEK 160
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL-------------EVRIDNL 941

                          170
                   ....*....|....*
gi 161082844   161 LQRLMDETRDLKQEL 175
Cdd:TIGR02168  942 QERLSEEYSLTLEEA 956
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-186 1.18e-04

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: 44.28  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    33 QEYDEFVEQSREMEIEMDATLDQKQSIIKDLTAKLTMFERENESLKLKLESHGIDMSnmEKQLETVKKDRDTMKVYLRQL 112
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEEL 452

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161082844   113 EQKNDDLERAHRILNESIENFEKMLDQAYEKNALLELEVDekgLLQEKLQRLMDETRDLKQELNVKSRFTPVVN 186
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLD---SLERLQENLEGFSEGVKALLKNQSGLSGILG 523
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-176 1.44e-04

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: 43.89  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    11 EDECRYWKERSKQYHKEWTDVKQE---YDEFVEQSREMEIEMDATLDQKQSIIKDLTAKLTMFERENESLKLKLESHGID 87
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    88 MSNMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKnalLELEVDEKGLLQEKLQRLMDE 167
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE---LEALLNERASLEEALALLRSE 895


                   ....*....
gi 161082844   168 TRDLKQELN 176
Cdd:TIGR02168  896 LEELSEELR 904
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 37-179 1.87e-04

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: 42.88  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   37 EFVEQSREMEIEMDAT---LDQKQSIIKDLTAKLTMFERENESLK---LKLESHGIDMSNMEKQLETVKKDRDTMKVYLr 110
Cdd:pfam15905 174 EVMAKQEGMEGKLQVTqknLEHSKGKVAQLEEKLVSTEKEKIEEKsetEKLLEYITELSCVSEQVEKYKLDIAQLEELL- 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  111 qlEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLELEVDEK-GLLQEKLQRLMDETRDLKQELNVKS 179
Cdd:pfam15905 253 --KEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELlREYEEKEQTLNAELEELKEKLTLEE 320
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 9-142 2.29e-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: 43.52  E-value: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844     9 SVEDECRYWKERSKQYHKEWTDVKQEYDEF-VEQSREME--IEMDATLDQKQSIIKDLTAKLTMFERENESLKLKLEShg 85
Cdd:TIGR02169  375 EVDKEFAETRDELKDYREKLEKLKREINELkRELDRLQEelQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK-- 452

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161082844    86 idmsnMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYE 142
Cdd:TIGR02169  453 -----QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 65-179 6.76e-04

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: 41.97  E-value: 6.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    65 AKLTMFERENESLKL--KLESHGIDMSNMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYE 142
Cdd:TIGR02168  668 TNSSILERRREIEELeeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 161082844   143 KNALLELEVDEKGLLQEKLQRLMDETRDLKQELNVKS 179
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-180 8.77e-04

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: 41.58  E-value: 8.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    33 QEYDEFVEQSREMEI--------EMDATLDQKQSIIKDLTAKLTMFERENESLKLKLESHGIDMSNMEKQLE-------T 97
Cdd:TIGR02168  213 ERYKELKAELRELELallvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844    98 VKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLELEVDEKGLLQEKLQRLMDETRDLKQELNV 177
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372


                   ...
gi 161082844   178 KSR 180
Cdd:TIGR02168  373 RLE 375
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-180 9.40e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 9.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   12 DECRYWKERSKQYHKEwtdvkQEYDEFVEQSREMEIEMDATLDQkqsiIKDLTAKLTMFERENESLKLKLESH-GIDMSN 90
Cdd:COG4913   272 AELEYLRAALRLWFAQ-----RRLELLEAELEELRAELARLEAE----LERLEARLDALREELDELEAQIRGNgGDRLEQ 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   91 MEKQLETVKKDRDTMKvylRQLEQKNDDLERAHRILNESIENFEKMLDQAyekNALLELEVDEKGLLQEKLQRLMDETRD 170
Cdd:COG4913   343 LEREIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRD 416

                         170
                  ....*....|
gi 161082844  171 LKQELNVKSR 180
Cdd:COG4913   417 LRRELRELEA 426
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 50-178 1.35e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  50 DATLDQKQSIIKDLTAKLTMFERENESLKLKLESHGIDMSNMEKQLETVKKDRDTMKvylRQLEQKNDDLERAHRILNES 129
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---AEIAEAEAEIEERREELGER 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161082844 130 I-------------------ENFEKMLDQA--------YEKNALLELEVDEKGL--LQEKLQRLMDETRDLKQELNVK 178
Cdd:COG3883   92 AralyrsggsvsyldvllgsESFSDFLDRLsalskiadADADLLEELKADKAELeaKKAELEAKLAELEALKAELEAA 169
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-176 2.28e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  27 EWTDVKQEYDEFVEQSREMEIEMD---ATLDQKQSIIKDLTAKLTMFERENESLKLKLESHGIDMSNMEKQLETVKKDRD 103
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEeleAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161082844 104 TMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLELEVDEKGLLQEKLQRLMDETRDLKQELN 176
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 30-241 2.78e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  30 DVKQEYDEFVEQSREMEIEMDAT---LDQKQSIIKDLTAKL-----TMFERENESLKLK--LESHGID------------ 87
Cdd:COG3883   48 ELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELgerarALYRSGGSVSYLDvlLGSESFSdfldrlsalski 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  88 MSNMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLELEVDEkglLQEKLQRLMDE 167
Cdd:COG3883  128 ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA---AEAQLAELEAE 204

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161082844 168 TRDLKQELNVKSRFTPVVNGTSVPTANDTNTVNSSMNSSASLPNGIVANGELVKHDNAVATRATSVSVNALNGS 241
Cdd:COG3883  205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
18-183 3.16e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  18 KERSKQYHKEWTDVKQEYDEFVEQSREMEIEMDATLDQKQSIiKDLTAKLTMFERENESLKLKLESHGIDMSNMEKQLET 97
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  98 VKKDRD--------------------TMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALL-ELEVDEKGL 156
Cdd:PRK03918 271 LKKEIEeleekvkelkelkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLeELKKKLKEL 350

                        170       180       190
                 ....*....|....*....|....*....|...
gi 161082844 157 LQ-----EKLQRLMDETRDLKQELN-VKSRFTP 183
Cdd:PRK03918 351 EKrleelEERHELYEEAKAKKEELErLKKRLTG 383
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 48-180 4.78e-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: 38.85  E-value: 4.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   48 EMDATLDQKQSIIKDLtakltmfERENESLKLKLESHGIDMSNMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILN 127
Cdd:TIGR04523 360 EKQRELEEKQNEIEKL-------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161082844  128 ESIENFEKMLDQAYEKNALLELEVDE----KGLLQEKLQRLMDETRDLKQELNVKSR 180
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNldntRESLETQLKVLSRSINKIKQNLEQKQK 489
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-175 5.70e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 5.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  19 ERSKQYHKEWTDVKQEYDEFVEQSREME---IEMDATLDQKQSIIKDLTAKLTMFERENESL---KLKLESHGIDMSNME 92
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEeliKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELE 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844  93 KQLETVKKDRDTMKVYLRQLEqknddlerahrilnESIENFEKMLDQAYEKNALLElEVDEKGLLQEKLQRLMDETRDLK 172
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELE--------------ERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309


                 ...
gi 161082844 173 QEL 175
Cdd:PRK03918 310 REI 312
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 30-177 7.71e-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: 38.46  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161082844   30 DVKQEYDEFVEQSREMEIEMDATLDQKQSIIKDLtakltmfERENESLKLKLESHGIDMSNMEKQLETVKKDRdtmkvyl 109
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK-------EKEKKDLIKEIEEKEKKISSLEKELEKAKKEN------- 626

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161082844  110 RQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLELEVDEkglLQEKLQRLMDETRDLKQELNV 177
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE---SKTKIDDIIELMKDWLKELSL 691
 
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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