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Conserved domains on  [gi|24653459|ref|NP_523732|]
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female lethal d, isoform A [Drosophila melanogaster]

Protein Classification

WTAP/Mum2p family protein( domain architecture ID 12181585)

WTAP/Mum2p (Wtap) family protein similar to Homo sapiens pre-mRNA-splicing regulator WTAP which is an associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 131-285 4.72e-66

WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.


:

Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 211.00  E-value: 4.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459   131 DAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAPTALALRTALLDPAVNLLFERLKKELKATKAKLEETQNELSAWKF 210
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653459   211 TPDSNTGKRLMAKCRLLYQENEELGKMTSNGRLAKLETELAMQKSFSEEVKKSQSELDDFLQELDEDVEGMQSTI 285
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
CwlO1 super family cl25603
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 247-335 2.33e-03

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


The actual alignment was detected with superfamily member COG3883:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 247 ETELAMQKSFSEEVKKSQSELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKD-----EVVAPA 321
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelGERARA 94

                        90
                ....*....|....
gi 24653459 322 AATNGGTNTTINKL 335
Cdd:COG3883  95 LYRSGGSVSYLDVL 108
 
Name Accession Description Interval E-value
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 131-285 4.72e-66

WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.


Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 211.00  E-value: 4.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459   131 DAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAPTALALRTALLDPAVNLLFERLKKELKATKAKLEETQNELSAWKF 210
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653459   211 TPDSNTGKRLMAKCRLLYQENEELGKMTSNGRLAKLETELAMQKSFSEEVKKSQSELDDFLQELDEDVEGMQSTI 285
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-319 4.65e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  111 LEDEIENLKlEQV----RMAQQCADAQRREKILmRRLANKEQEFQDYVSQIAEYKAQQAPTAL---ALRTALLDPAVnll 183
Cdd:COG4913  223 TFEAADALV-EHFddleRAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLwfaQRRLELLEAEL--- 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  184 fERLKKELKATKAKLEETQNELSAwkftpdsntgkrLMAKCRLLYQENEELGkmtsNGRLAKLETELAMQKSFSEEVKKS 263
Cdd:COG4913  298 -EELRAELARLEAELERLEARLDA------------LREELDELEAQIRGNG----GDRLEQLEREIERLERELEERERR 360

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24653459  264 QSELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKDEVVA 319
Cdd:COG4913  361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 111-324 5.83e-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: 5.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    111 LEDEIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAP--TALALRTALLDPAVNLL----- 183
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKltEEYAELKEELEDLRAELeevdk 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    184 -FERLKKELKATKAKLEETQNELSAWKFTPDsntgkRLMAKCRLLYQENEEL-GKMTS-NGRLAKLETELamqKSFSEEV 260
Cdd:TIGR02169  379 eFAETRDELKDYREKLEKLKREINELKRELD-----RLQEELQRLSEELADLnAAIAGiEAKINELEEEK---EDKALEI 450

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653459    261 KKSQSElddfLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQL---KQAIKDEVVAPAAAT 324
Cdd:TIGR02169  451 KKQEWK----LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaqARASEERVRGGRAVE 513
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 247-335 2.33e-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: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 247 ETELAMQKSFSEEVKKSQSELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKD-----EVVAPA 321
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelGERARA 94

                        90
                ....*....|....
gi 24653459 322 AATNGGTNTTINKL 335
Cdd:COG3883  95 LYRSGGSVSYLDVL 108
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
107-325 2.83e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  107 RQRLLEDEIENLKLEQVRmaQQCADAqrreKILMRR-LANKEQEFQDYVSQIAEYKAQQAPTAL-ALRTALLDpaVNLLF 184
Cdd:PRK02224 151 RQDMIDDLLQLGKLEEYR--ERASDA----RLGVERvLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAE--LDEEI 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  185 ERLKKELKATKAKLEETQNELSAWKftpdsntGKRlmakcrllyQENEELGKMTSNGRLAKLETElAMQKSFSEEVkksq 264
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHE-------ERR---------EELETLEAEIEDLRETIAETE-REREELAEEV---- 281

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24653459  265 SELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKDEVVAPAAATN 325
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
 
Name Accession Description Interval E-value
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 131-285 4.72e-66

WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.


Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 211.00  E-value: 4.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459   131 DAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAPTALALRTALLDPAVNLLFERLKKELKATKAKLEETQNELSAWKF 210
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653459   211 TPDSNTGKRLMAKCRLLYQENEELGKMTSNGRLAKLETELAMQKSFSEEVKKSQSELDDFLQELDEDVEGMQSTI 285
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-319 4.65e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  111 LEDEIENLKlEQV----RMAQQCADAQRREKILmRRLANKEQEFQDYVSQIAEYKAQQAPTAL---ALRTALLDPAVnll 183
Cdd:COG4913  223 TFEAADALV-EHFddleRAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLwfaQRRLELLEAEL--- 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  184 fERLKKELKATKAKLEETQNELSAwkftpdsntgkrLMAKCRLLYQENEELGkmtsNGRLAKLETELAMQKSFSEEVKKS 263
Cdd:COG4913  298 -EELRAELARLEAELERLEARLDA------------LREELDELEAQIRGNG----GDRLEQLEREIERLERELEERERR 360

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24653459  264 QSELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKDEVVA 319
Cdd:COG4913  361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 111-324 5.83e-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: 5.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    111 LEDEIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAP--TALALRTALLDPAVNLL----- 183
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKltEEYAELKEELEDLRAELeevdk 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    184 -FERLKKELKATKAKLEETQNELSAWKFTPDsntgkRLMAKCRLLYQENEEL-GKMTS-NGRLAKLETELamqKSFSEEV 260
Cdd:TIGR02169  379 eFAETRDELKDYREKLEKLKREINELKRELD-----RLQEELQRLSEELADLnAAIAGiEAKINELEEEK---EDKALEI 450

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653459    261 KKSQSElddfLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQL---KQAIKDEVVAPAAAT 324
Cdd:TIGR02169  451 KKQEWK----LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaqARASEERVRGGRAVE 513
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 109-315 5.33e-06

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: 49.30  E-value: 5.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    109 RLLEDEIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAptalALRTALLDPAVNLLFERLK 188
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH----KLEEALNDLEARLSHSRIP 794

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    189 kELKATKAKLEETQNELSAwkftpdsntgkrlmakcRLlyqenEELgkmtsNGRLAKLETELAMQKSFSEEVKKSQSELD 268
Cdd:TIGR02169  795 -EIQAELSKLEEEVSRIEA-----------------RL-----REI-----EQKLNRLTLEKEYLEKEIQELQEQRIDLK 846

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 24653459    269 DFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKD 315
Cdd:TIGR02169  847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 107-323 7.29e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 7.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 107 RQRLLEDEIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQaptalalrtalldpavnllfER 186
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL--------------------EE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 187 LKKELKATKAKLEETQNELSAWKftpdsntgkrlmAKCRLLYQENEELGKmtsngRLAKLETELAMQKSFSEEVKKSQSE 266
Cdd:COG1196 321 LEEELAELEEELEELEEELEELE------------EELEEAEEELEEAEA-----ELAEAEEALLEAEAELAEAEEELEE 383

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24653459 267 LDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKDEVVAPAAA 323
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-337 1.08e-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: 48.51  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    109 RLLEDEIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQA---PTALALRTALLDPAVNLlfE 185
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleAELEELESRLEELEEQL--E 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    186 RLKKELKATKAKLEETQNELSAWKftpdsNTGKRLMAKCRLLYQENEELGKMTSNGRLAKLETELAMQKSFSEEVKKSQS 265
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLE-----ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24653459    266 ELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEK--ENAQLKQAIKDEVVAPAAATNGGTNTTINKLET 337
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlqENLEGFSEGVKALLKNQSGLSGILGVLSELISV 531
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 111-325 3.75e-05

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: 45.91  E-value: 3.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 111 LEDEIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAptalALRTALldpavnllfERLKKE 190
Cdd:COG4942  25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAEL---------AELEKE 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 191 LKATKAKLEETQNELS-----AWK----------FTPDS--NTGKRLMAKCRLLYQENEELGKMTSN-GRLAKLETELAM 252
Cdd:COG4942  92 IAELRAELEAQKEELAellraLYRlgrqpplallLSPEDflDAVRRLQYLKYLAPARREQAEELRADlAELAALRAELEA 171

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653459 253 QKsfsEEVKKSQSELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKDEVVAPAAATN 325
Cdd:COG4942 172 ER---AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 107-315 1.09e-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: 45.05  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    107 RQRLLEDEIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAPTALALRTALLDPavnllfER 186
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL------DE 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    187 LKKELKATKAKLEETQNELSAWKFTPDSNTGKRLMAKCRLLYQENE-----------ELGKMTSNGRLAKLETELAMQKS 255
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQletlrskvaqlELQIASLNNEIERLEARLERLED 414

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653459    256 FSEEVKKSQSELDDFLQ-----ELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKD 315
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-324 1.23e-03

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: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    114 EIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAPTALALRTALLD-PAVNLLFERLKKELK 192
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEvEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    193 ATKAKLEETQNELsawkftpdsntgkrlmAKCRLLYQENEElGKMTSNGRLAKLETELAMQKSFSEEVKKSQSELDDFLQ 272
Cdd:TIGR02168  758 ELEAEIEELEERL----------------EEAEEELAEAEA-EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24653459    273 ELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKDEVVAPAAAT 324
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
130-311 1.47e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 130 ADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAPTALALRTALLDPAVNllfeRLKKELKATKAKLEETQNELSAWK 209
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLS----ELESQLAEARAELAEAEARLAALR 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 210 ftpdSNTGKRLMAKCRLLyqENEELGKMTSngRLAKLETELA-MQKSFSEE---VKKSQSELDDFLQELDE--------- 276
Cdd:COG3206 247 ----AQLGSGPDALPELL--QSPVIQQLRA--QLAELEAELAeLSARYTPNhpdVIALRAQIAALRAQLQQeaqrilasl 318

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24653459 277 --DVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQ 311
Cdd:COG3206 319 eaELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 247-335 2.33e-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: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 247 ETELAMQKSFSEEVKKSQSELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKD-----EVVAPA 321
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelGERARA 94

                        90
                ....*....|....
gi 24653459 322 AATNGGTNTTINKL 335
Cdd:COG3883  95 LYRSGGSVSYLDVL 108
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 107-323 2.46e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 107 RQRLLEDEIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAPTALALRTAL--LDPAVNLLF 184
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEaeLAEAEEELE 382

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 185 ERLKKELKATKAKLEETQNELSAwkftpdSNTGKRLMAKCRLLYQENEELgkmtsNGRLAKLETELAMQKSFSEEVKKSQ 264
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEEL------EEAEEALLERLERLEEELEEL-----EEALAELEEEEEEEEEALEEAAEEE 451

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24653459 265 SELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKDEVVAPAAA 323
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
107-325 2.83e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  107 RQRLLEDEIENLKLEQVRmaQQCADAqrreKILMRR-LANKEQEFQDYVSQIAEYKAQQAPTAL-ALRTALLDpaVNLLF 184
Cdd:PRK02224 151 RQDMIDDLLQLGKLEEYR--ERASDA----RLGVERvLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAE--LDEEI 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  185 ERLKKELKATKAKLEETQNELSAWKftpdsntGKRlmakcrllyQENEELGKMTSNGRLAKLETElAMQKSFSEEVkksq 264
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHE-------ERR---------EELETLEAEIEDLRETIAETE-REREELAEEV---- 281

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24653459  265 SELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKDEVVAPAAATN 325
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
185-317 3.19e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 3.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 185 ERLKKELKATKAKLEETQNELSAWKFTPDSNTGKRLMAKCRLLYQENEELgkmtsNGRLAKLEtelamqksfsEEVKKSQ 264
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEEL-----EAELEEKD----------ERIERLE 447

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24653459 265 SELDDFLQEL------DEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKDEV 317
Cdd:COG2433 448 RELSEARSEErreirkDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 107-315 3.80e-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: 40.00  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459   107 RQRLLEDEIENLKLEQvrmaqqcadaqrreKILMRRLANKEQEFQDYVSQIAEYKAQqaptalalrtalldpavnllFER 186
Cdd:TIGR04523 212 KNKSLESQISELKKQN--------------NQLKDNIEKKQQEINEKTTEISNTQTQ--------------------LNQ 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459   187 LKKELKATKAKLEETQNELSawkftpdsNTGKRLMAKCRLLYQ---ENEELGKMTSNGRLAKLETELAMQKSFSEEVK-- 261
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELE--------QNNKKIKELEKQLNQlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQnq 329

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24653459   262 -----KSQSELDDFLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQAIKD 315
Cdd:TIGR04523 330 isqnnKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-319 4.21e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  131 DAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAptALALRTALLDPAVNLLFERLkkELKATKAKLEETQNELsawkf 210
Cdd:COG4913  607 DNRAKLAALEAELAELEEELAEAEERLEALEAELD--ALQERREALQRLAEYSWDEI--DVASAEREIAELEAEL----- 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459  211 tpdsntgKRLMAkcrllyqeneelgkmtSNGRLAKLETELamqksfsEEVKKSQSELDDFLQELDEDVEGMQSTILFLQQ 290
Cdd:COG4913  678 -------ERLDA----------------SSDDLAALEEQL-------EELEAELEELEEELDELKGEIGRLEKELEQAEE 727

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 24653459  291 ELKTTRDRIQTLEKE---------NAQLKQAIKDEVVA 319
Cdd:COG4913  728 ELDELQDRLEAAEDLarlelrallEERFAAALGDAVER 765
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 118-309 5.44e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.34  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459   118 LKLEQVRMAQQCADAQRREKILMRRLANKeqeFQDYVSQIAEYKAQQAPTALALRTALLDPAVNL--LFERLKKELKATK 195
Cdd:pfam05557  55 KRIRLLEKREAEAEEALREQAELNRLKKK---YLEALNKKLNEKESQLADAREVISCLKNELSELrrQIQRAELELQSTN 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459   196 AKLEETQNELsawkftpdsntgKRLMAKCRLLYQENEELGKMTS-----NGRLAKLETELAMQKSFSEEVKKSQSELDDF 270
Cdd:pfam05557 132 SELEELQERL------------DLLKAKASEAEQLRQNLEKQQSslaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 24653459   271 ------LQELDEDVEGMQSTI---LFLQQELKTTRDRIQTLEKENAQL 309
Cdd:pfam05557 200 pelekeLERLREHNKHLNENIenkLLLKEEVEDLKRKLEREEKYREEA 247
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 107-312 5.54e-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: 39.36  E-value: 5.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 107 RQRLLEDEIENLKLEQVRMAQQCADAQRREKILMRRLANKEQEFQDYVSQIAEYKAQQAPTALALRTALLDPAVNLL--- 183
Cdd:COG4942  49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLlsp 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459 184 --FERLKKELKATKAKLEETQNELSAWKftpdsNTGKRLMAKCRLLYQENEELgkmtsngrlAKLETELAMQKSFSEEVK 261
Cdd:COG4942 129 edFLDAVRRLQYLKYLAPARREQAEELR-----ADLAELAALRAELEAERAEL---------EALLAELEEERAALEALK 194

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24653459 262 KSQSELddfLQELDEDVEGMQSTILFLQQELKTTRDRIQTLEKENAQLKQA 312
Cdd:COG4942 195 AERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 111-319 5.87e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    111 LEDEIENLKLEQVRMAQQCADAQRREKilmrRLANKEQEFQDYVSQiAEYKAQQAPTALALRTALLDPAVNLLFE----- 185
Cdd:pfam01576  382 LESENAELQAELRTLQQAKQDSEHKRK----KLEGQLQELQARLSE-SERQRAELAEKLSKLQSELESVSSLLNEaegkn 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653459    186 -RLKKELKATKAKLEETQNELSawkftpdSNTGKRLMAKCRLLYQENEElgkmtsNGRLAKLETELAMQKSFSEEVKKSQ 264
Cdd:pfam01576  457 iKLSKDVSSLESQLQDTQELLQ-------EETRQKLNLSTRLRQLEDER------NSLQEQLEEEEEAKRNVERQLSTLQ 523

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653459    265 SELDDFLQELDED---VEGMQSTILFLQQELKTTRDRIQT-------LEKENAQLKQAIKDEVVA 319
Cdd:pfam01576  524 AQLSDMKKKLEEDagtLEALEEGKKRLQRELEALTQQLEEkaaaydkLEKTKNRLQQELDDLLVD 588
 
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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