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Conserved domains on  [gi|530383030|ref|XP_005248722|]
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lebercilin isoform X1 [Homo sapiens]

Protein Classification

Lebercilin domain-containing protein( domain architecture ID 12174059)

Lebercilin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 100-292 4.70e-67

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


:

Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 218.62  E-value: 4.70e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  100 VTKRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQ 179
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  180 EKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLA 259
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 530383030  260 ERKRAYEAHDENKVLQKEVQRLYHKLKEKEREL 292
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
PTZ00121 super family cl31754
MAEBL; Provisional
 90-482 2.14e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   90 REPLRKDTDLVTKRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKA--LNKFEDAENEISQLIfRHNNE 167
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAK-KKAEE 1429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  168 ITALKERLRKSQEKERATEKRVKDTESElfRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLE 247
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAK--KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  248 LSTNSFQRQLLAERKRAYEAHDENKVLQKEVQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKNAACQSDFA- 326
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAk 1587

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  327 -------DLCTKGVQTMEDFKPEEYPLTPETIMCYEN--KWEEPGHLTLDLQSQKQDRHGEAGILNPimEREEKFVTDEE 397
Cdd:PTZ00121 1588 kaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAE 1665

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  398 LHVVKQEVEKLEDEWEREELDKKQKEKASLLEREEKPEWETGRYQLGMYPIQNMDKLQGEEEERLKREMLLAKLNEIDRE 477
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745


                  ....*
gi 530383030  478 LQDSR 482
Cdd:PTZ00121 1746 AEEAK 1750
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 100-292 4.70e-67

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 218.62  E-value: 4.70e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  100 VTKRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQ 179
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  180 EKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLA 259
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 530383030  260 ERKRAYEAHDENKVLQKEVQRLYHKLKEKEREL 292
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 105-328 9.26e-10

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: 60.93  E-value: 9.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 105 LSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERA 184
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 185 TEKRVKDTESELFRTKFSLQKLKEISEARHL--------------------PERDDLAKKLVSAELKLDDTERRIKELSK 244
Cdd:COG4942   95 LRAELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 245 NLElstnSFQRQLLAERKRAYEAHDENKVLQKEVQRlyhKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKNAACQSD 324
Cdd:COG4942  175 ELE----ALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247


                 ....
gi 530383030 325 FADL 328
Cdd:COG4942  248 FAAL 251
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 111-435 2.09e-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: 54.69  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   111 KINELQNEVSELQVKLAELLKENKSL-KRLQYRQEKaLNKFEDAENEISQLIFRHnnEITALKERLRKSQEKERATEKRV 189
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELeARIEELEED-LHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEARL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   190 KDTESELFRTKFSLQKLKEisearhlpERDDLAKKLVSAELKLDDTERRIKELSKNLElstnSFQRQLLAERKRAYEAHD 269
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEK--------EIQELQEQRIDLKEQIKSIEKEIENLNGKKE----ELEEELEELEAALRDLES 882

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   270 ENKVLQKEVQRLYHKLKEKERELDIKNIysnrlpksSPNKEKELALRKNAACQSDFADLctkgvQTMEDFKPEEYPlTPE 349
Cdd:TIGR02169  883 RLGDLKKERDELEAQLRELERKIEELEA--------QIEKKRKRLSELKAKLEALEEEL-----SEIEDPKGEDEE-IPE 948

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   350 TIMCYEnkweepghltlDLQSQKQDRHGEAGILNPI-MEREEKFvtdeelhvvkQEVEKLEDEWErEELDKKQKEKASLL 428
Cdd:TIGR02169  949 EELSLE-----------DVQAELQRVEEEIRALEPVnMLAIQEY----------EEVLKRLDELK-EKRAKLEEERKAIL 1006


                   ....*..
gi 530383030   429 EREEKPE 435
Cdd:TIGR02169 1007 ERIEEYE 1013
PTZ00121 PTZ00121
MAEBL; Provisional
 90-482 2.14e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   90 REPLRKDTDLVTKRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKA--LNKFEDAENEISQLIfRHNNE 167
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAK-KKAEE 1429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  168 ITALKERLRKSQEKERATEKRVKDTESElfRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLE 247
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAK--KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  248 LSTNSFQRQLLAERKRAYEAHDENKVLQKEVQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKNAACQSDFA- 326
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAk 1587

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  327 -------DLCTKGVQTMEDFKPEEYPLTPETIMCYEN--KWEEPGHLTLDLQSQKQDRHGEAGILNPimEREEKFVTDEE 397
Cdd:PTZ00121 1588 kaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAE 1665

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  398 LHVVKQEVEKLEDEWEREELDKKQKEKASLLEREEKPEWETGRYQLGMYPIQNMDKLQGEEEERLKREMLLAKLNEIDRE 477
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745


                  ....*
gi 530383030  478 LQDSR 482
Cdd:PTZ00121 1746 AEEAK 1750
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 108-298 7.46e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.07  E-value: 7.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 108 RLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQ-----EKALNKFEDAENEISQLIFRHNNEITALKERLRK-SQEK 181
Cdd:PRK05771  44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVsvkslEELIKDVEEELEKIEKEIKELEEEISELENEIKElEQEI 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 182 ERAteKRVKDTESE---LFRTKFSLQKLKEISEArHLPERDDLAKKLVSAELKLDDTERRI-----KELSKNL--ELSTN 251
Cdd:PRK05771 124 ERL--EPWGNFDLDlslLLGFKYVSVFVGTVPED-KLEELKLESDVENVEYISTDKGYVYVvvvvlKELSDEVeeELKKL 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530383030 252 SFQRQLLAERKRAYEA----HDENKVLQKEVQRLYHKLKE--KERELDIKNIY 298
Cdd:PRK05771 201 GFERLELEEEGTPSELireiKEELEEIEKERESLLEELKElaKKYLEELLALY 253
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 100-292 4.70e-67

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 218.62  E-value: 4.70e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  100 VTKRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQ 179
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  180 EKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLA 259
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 530383030  260 ERKRAYEAHDENKVLQKEVQRLYHKLKEKEREL 292
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 105-328 9.26e-10

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: 60.93  E-value: 9.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 105 LSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERA 184
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 185 TEKRVKDTESELFRTKFSLQKLKEISEARHL--------------------PERDDLAKKLVSAELKLDDTERRIKELSK 244
Cdd:COG4942   95 LRAELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 245 NLElstnSFQRQLLAERKRAYEAHDENKVLQKEVQRlyhKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKNAACQSD 324
Cdd:COG4942  175 ELE----ALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247


                 ....
gi 530383030 325 FADL 328
Cdd:COG4942  248 FAAL 251
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 111-435 2.09e-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: 54.69  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   111 KINELQNEVSELQVKLAELLKENKSL-KRLQYRQEKaLNKFEDAENEISQLIFRHnnEITALKERLRKSQEKERATEKRV 189
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELeARIEELEED-LHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEARL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   190 KDTESELFRTKFSLQKLKEisearhlpERDDLAKKLVSAELKLDDTERRIKELSKNLElstnSFQRQLLAERKRAYEAHD 269
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEK--------EIQELQEQRIDLKEQIKSIEKEIENLNGKKE----ELEEELEELEAALRDLES 882

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   270 ENKVLQKEVQRLYHKLKEKERELDIKNIysnrlpksSPNKEKELALRKNAACQSDFADLctkgvQTMEDFKPEEYPlTPE 349
Cdd:TIGR02169  883 RLGDLKKERDELEAQLRELERKIEELEA--------QIEKKRKRLSELKAKLEALEEEL-----SEIEDPKGEDEE-IPE 948

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   350 TIMCYEnkweepghltlDLQSQKQDRHGEAGILNPI-MEREEKFvtdeelhvvkQEVEKLEDEWErEELDKKQKEKASLL 428
Cdd:TIGR02169  949 EELSLE-----------DVQAELQRVEEEIRALEPVnMLAIQEY----------EEVLKRLDELK-EKRAKLEEERKAIL 1006


                   ....*..
gi 530383030   429 EREEKPE 435
Cdd:TIGR02169 1007 ERIEEYE 1013
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 111-292 1.06e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 111 KINELQNEVSELQVKLAELLKEnksLKRLQYRQEKALNKFEDAENEISQLifrhNNEITALKERLRKSQEKeraTEKRVK 190
Cdd:COG3883   24 ELSELQAELEAAQAELDALQAE---LEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREE---LGERAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 191 DteseLFRTKFSLQKLKEISEARHLPE---RDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLAERKRAYEA 267
Cdd:COG3883   94 A----LYRSGGSVSYLDVLLGSESFSDfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169

                        170       180
                 ....*....|....*....|....*
gi 530383030 268 HDENKVLQKEVQRLYHKLKEKEREL 292
Cdd:COG3883  170 KAELEAQQAEQEALLAQLSAEEAAA 194
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
105-239 1.43e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  105 LSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQL---IFRHNNEITALKERLRKSQEK 181
Cdd:COG4913   656 YSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELkgeIGRLEKELEQAEEELDELQDR 735

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530383030  182 ERATEKRVKDTESELFRTKFSlqklKEISEARHLPERDDLAKKLVSAELKLDDTERRI 239
Cdd:COG4913   736 LEAAEDLARLELRALLEERFA----AALGDAVERELRENLEERIDALRARLNRAEEEL 789
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 111-292 1.92e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 111 KINELQNEVSELQVKL----AELLKENKSLKRLQYRQEKALNKFEDAENEISQLIfrhnNEITALKERLRKSQEKERATE 186
Cdd:COG1196  247 ELEELEAELEELEAELaeleAELEELRLELEELELELEEAQAEEYELLAELARLE----QDIARLEERRRELEERLEELE 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 187 KRVKDTESELFRTKFSLQKLKEiSEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLElstnSFQRQLLAERKRAYE 266
Cdd:COG1196  323 EELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE----ELAEELLEALRAAAE 397

                        170       180
                 ....*....|....*....|....*.
gi 530383030 267 AHDENKVLQKEVQRLYHKLKEKEREL 292
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEEL 423
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 93-293 4.33e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  93 LRKDTDLVTKRILSARLlKINELQNEVSELQVKLAELLKE----NKSLKRLQYRQEKALNKFEDAENEISQLIFRHNN-- 166
Cdd:COG1196  258 LEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAElarlEQDIARLEERRRELEERLEELEEELAELEEELEEle 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 167 --------EITALKERLRKSQEKERATEKRVKDTESELfRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERR 238
Cdd:COG1196  337 eeleeleeELEEAEEELEEAEAELAEAEEALLEAEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530383030 239 IKELSKNLElstnSFQRQLLAERKRAYEAHDENKVLQKEVQRLYHKLKEKERELD 293
Cdd:COG1196  416 LERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-293 5.26e-06

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: 50.06  E-value: 5.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   111 KINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNkfeDAENEISQLifrhNNEITALKERLRKSQEKERATEKRVK 190
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY---ALANEISRL----EQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   191 DTESELFRTKFSLQKLKEISEaRHLPERDDLAKKLVSAELKLDDTERRIKELSKNLE-LSTNSFQ--RQLLAERKRAYEA 267
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQleLQIASLNNEIERL 405

                          170       180
                   ....*....|....*....|....*.
gi 530383030   268 HDENKVLQKEVQRLYHKLKEKERELD 293
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEELLKKLE 431
PTZ00121 PTZ00121
MAEBL; Provisional
 90-482 2.14e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   90 REPLRKDTDLVTKRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKA--LNKFEDAENEISQLIfRHNNE 167
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAK-KKAEE 1429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  168 ITALKERLRKSQEKERATEKRVKDTESElfRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLE 247
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAK--KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  248 LSTNSFQRQLLAERKRAYEAHDENKVLQKEVQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKNAACQSDFA- 326
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAk 1587

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  327 -------DLCTKGVQTMEDFKPEEYPLTPETIMCYEN--KWEEPGHLTLDLQSQKQDRHGEAGILNPimEREEKFVTDEE 397
Cdd:PTZ00121 1588 kaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAE 1665

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  398 LHVVKQEVEKLEDEWEREELDKKQKEKASLLEREEKPEWETGRYQLGMYPIQNMDKLQGEEEERLKREMLLAKLNEIDRE 477
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745


                  ....*
gi 530383030  478 LQDSR 482
Cdd:PTZ00121 1746 AEEAK 1750
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 108-298 7.46e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.07  E-value: 7.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 108 RLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQ-----EKALNKFEDAENEISQLIFRHNNEITALKERLRK-SQEK 181
Cdd:PRK05771  44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVsvkslEELIKDVEEELEKIEKEIKELEEEISELENEIKElEQEI 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 182 ERAteKRVKDTESE---LFRTKFSLQKLKEISEArHLPERDDLAKKLVSAELKLDDTERRI-----KELSKNL--ELSTN 251
Cdd:PRK05771 124 ERL--EPWGNFDLDlslLLGFKYVSVFVGTVPED-KLEELKLESDVENVEYISTDKGYVYVvvvvlKELSDEVeeELKKL 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530383030 252 SFQRQLLAERKRAYEA----HDENKVLQKEVQRLYHKLKE--KERELDIKNIY 298
Cdd:PRK05771 201 GFERLELEEEGTPSELireiKEELEEIEKERESLLEELKElaKKYLEELLALY 253
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 102-196 9.06e-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: 45.53  E-value: 9.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 102 KRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEK 181
Cdd:COG4942  142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221

                         90
                 ....*....|....*
gi 530383030 182 ERATEKRVKDTESEL 196
Cdd:COG4942  222 AEELEALIARLEAEA 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 105-293 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: 45.82  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   105 LSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKAL----NKFEDAENEISQL---IFRHNNEITALKERLRK 177
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELeaqLEELESKLDELAEELAE 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   178 SQEKERATEKRVKDTESELFRTKFSLQKLKEISE-------------ARHLPERDDLAKKLVSAELKLDDTERRIKELSK 244
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEeleeqletlrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 530383030   245 NLELSTNSFQRQLLAERKRAYEAHDENKV-LQKEVQRLYHKLKEKERELD 293
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQAELEELEEELEeLQEELERLEEALEELREELE 471
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 107-288 1.47e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 107 ARLLKINELQNEVSELQVKLAELLKEnksLKRLQYRQEKALNKFEDAENEISQL---IFRHNNEITALKERLRKSQEK-- 181
Cdd:COG1579    7 RALLDLQELDSELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELEDLekeIKRLELEIEEVEARIKKYEEQlg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 182 ERATEKRVKDTESELFRTKfSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQ---LL 258
Cdd:COG1579   84 NVRNNKEYEALQKEIESLK-RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEleeLE 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 530383030 259 AERKRAYEAhdenkvLQKEVQRLYHKLKEK 288
Cdd:COG1579  163 AEREELAAK------IPPELLALYERIRKR 186
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
84-319 1.61e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  84 RSQSLNREPLRKDTDLVTKRIlsarllkiNELQNEVSELQVKLAellkenkslkrlQYRQEKALNKFEDAENEISQLIFR 163
Cdd:COG3206  164 QNLELRREEARKALEFLEEQL--------PELRKELEEAEAALE------------EFRQKNGLVDLSEEAKLLLQQLSE 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 164 HNNEITALKERLRKSQEKERATEKRVKDTESELFRTKFS--LQKLK-EISEARHlpERDDLAKKL-------VSAELKLD 233
Cdd:COG3206  224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRaQLAELEA--ELAELSARYtpnhpdvIALRAQIA 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 234 DTERRIKELSKNLELSTNSfQRQLLAERKRAYEAhdENKVLQKEVQRL---YHKLKEKERELDI-KNIYSNRLpksspNK 309
Cdd:COG3206  302 ALRAQLQQEAQRILASLEA-ELEALQAREASLQA--QLAQLEARLAELpelEAELRRLEREVEVaRELYESLL-----QR 373

                        250
                 ....*....|
gi 530383030 310 EKELALRKNA 319
Cdd:COG3206  374 LEEARLAEAL 383
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 111-316 2.01e-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: 44.67  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   111 KINELQNEVSELQVKLAELLKENKSLKRLQYRQEKalnKFEDAENEISQLifrhNNEITALKERLRKSQEKERATEKRVK 190
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASR---KIGEIEKEIEQL----EQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   191 DTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLlaERKRAYEAHDE 270
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL--NRLTLEKEYLE 832

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 530383030   271 NKVLQKEVQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELALR 316
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 112-314 4.52e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 112 INELQNEVSELQVKLAELLKEnksLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERATEKRVKD 191
Cdd:COG1196  325 LAELEEELEELEEELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 192 TESELfrtkfSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLElstNSFQRQLLAERKRAYEAHDEN 271
Cdd:COG1196  402 LEELE-----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA---ELEEEEEALLELLAELLEEAA 473

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530383030 272 KVLQKEVQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELA 314
Cdd:COG1196  474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 97-424 4.81e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.42  E-value: 4.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030    97 TDLVTKRILSARLLKINELQNEVSELQ-VKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNE-ITALKER 174
Cdd:pfam02463  687 SELAKEEILRRQLEIKKKEQREKEELKkLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKkEEKEEEK 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   175 LRKSQEKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQ 254
Cdd:pfam02463  767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   255 RQLLAERKRAYEAHDENKVLQKEVQRLYHKLKEKERELDIKNIYSNRLPKsspNKEKELALRKNAACQSDFADLCTKGVQ 334
Cdd:pfam02463  847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK---EEKKELEEESQKLNLLEEKENEIEERI 923

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   335 TMEDFKPEEYPLTPETIMCYENKWEEPGHLTLDLQSQKQDRHGEAGIL------NPIMEREEKFVTDEELHVVKQEVEKL 408
Cdd:pfam02463  924 KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEElgkvnlMAIEEFEEKEERYNKDELEKERLEEE 1003

                          330
                   ....*....|....*.
gi 530383030   409 EDEWEREELDKKQKEK 424
Cdd:pfam02463 1004 KKKLIRAIIEETCQRL 1019
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-293 8.13e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  108 RLLKINELQNEVSELQVKLAELlkeNKSLKRLQ-YRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERATE 186
Cdd:COG4913   253 LLEPIRELAERYAAARERLAEL---EYLRAALRlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  187 --------KRVKDTESELfrtkfslqKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLElstnSFQRQLL 258
Cdd:COG4913   330 aqirgnggDRLEQLEREI--------ERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA----ALLEALE 397

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530383030  259 AERKRAYEAHDENKVLQKEVQRlyhKLKEKERELD 293
Cdd:COG4913   398 EELEALEEALAEAEAALRDLRR---ELRELEAEIA 429
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
114-293 8.49e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 8.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 114 ELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQlifrHNNEITALKERLRKSQEKERATEKRVKDTE 193
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELE 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 194 SELFRTKFSLQKLKE-ISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQlLAERKRAYEAHDENK 272
Cdd:PRK03918 266 ERIEELKKEIEELEEkVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELK 344

                        170       180
                 ....*....|....*....|.
gi 530383030 273 VLQKEVQRLYHKLKEKERELD 293
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYE 365
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-293 9.81e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 9.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  111 KINELQNEVSELQVKLAELLKENKSLKrlqyRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERATEkrvk 190
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDA---- 682

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  191 dTESELFRTKFSLQKLK-EISEARHlpERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLAERKRAYEAHD 269
Cdd:COG4913   683 -SSDDLAALEEQLEELEaELEELEE--ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759

                         170       180
                  ....*....|....*....|....
gi 530383030  270 ENKVLQKEVQRLYHKLKEKERELD 293
Cdd:COG4913   760 GDAVERELRENLEERIDALRARLN 783
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
105-482 1.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 105 LSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQL----IFRHNNEITALKERLRKSQE 180
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltPEKLEKELEELEKAKEEIEE 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 181 KERATEKRVKDTESELFRTKFSLQKLK-----------EISE-------ARHLPERDDLAKKLVSAELKLDDTERRIKEL 242
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrELTEehrkellEEYTAELKRIEKELKEIEEKERKLRKELREL 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 243 SKNLELSTNSFQRQLLAERKRAYEAHDENKVLQK--EVQRLYHKLKEKEREL--DIKNIYSNRLPKSSPNKEKELALRKN 318
Cdd:PRK03918 486 EKVLKKESELIKLKELAEQLKELEEKLKKYNLEEleKKAEEYEKLKEKLIKLkgEIKSLKKELEKLEELKKKLAELEKKL 565

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 319 AACQSDFADLCTK----GVQTMEDFKPEEYPLTPetimcYENKWEEPGHLTLDLQSQKQDRHGEAGILNpiMEREEKFVT 394
Cdd:PRK03918 566 DELEEELAELLKEleelGFESVEELEERLKELEP-----FYNEYLELKDAEKELEREEKELKKLEEELD--KAFEELAET 638

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 395 DEELHVVKQEVEKLEDEWEREELDKKQKEKASLLE-----REEKPEWETGRYQLgmypIQNMDKLQGEEEERLKREMLLA 469
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEELREEYLELSRelaglRAELEELEKRREEI----KKTLEKLKEELEEREKAKKELE 714

                        410
                 ....*....|...
gi 530383030 470 KLNEIDRELQDSR 482
Cdd:PRK03918 715 KLEKALERVEELR 727
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
103-267 1.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 103 RILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAEnEISQLifrhNNEITALKERLRKSQEKE 182
Cdd:COG4717   81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-ELEAL----EAELAELPERLEELEERL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 183 RA---TEKRVKDTESELFRTKFSLQKLKEISEA-------RHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNS 252
Cdd:COG4717  156 EElreLEEELEELEAELAELQEELEELLEQLSLateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235

                        170
                 ....*....|....*
gi 530383030 253 FQRQLLAERKRAYEA 267
Cdd:COG4717  236 LEAAALEERLKEARL 250
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 111-318 1.84e-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: 41.54  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  111 KINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERATEKRVK 190
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  191 DTESELFRTKFSLQKLKEISEARHlPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFqrqllaeRKRAYEAHDE 270
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNN-SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI-------NKIKQNLEQK 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 530383030  271 NKVLQKEVQRLyHKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKN 318
Cdd:TIGR04523 488 QKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 99-320 2.47e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   99 LVTKRILSARLLKINELQNEVSELQVKLAELLKE------NKSLKRLqyrqEKALNKFEDAENEISQLIFRHNNEITALK 172
Cdd:PTZ00108 1091 LLSMPIWSLTKEKVEKLNAELEKKEKELEKLKNTtpkdmwLEDLDKF----EEALEEQEEVEEKEIAKEQRLKSKTKGKA 1166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  173 ERLRKSQEKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNS 252
Cdd:PTZ00108 1167 SKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSK 1246

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530383030  253 fqrqllaerkrayEAHDENKVLQKEVQRLYHKLKEKERELDIKNI----YSNRLPKSSPNKEKELALRKNAA 320
Cdd:PTZ00108 1247 -------------KNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVsavqYSPPPPSKRPDGESNGGSKPSSP 1305
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-293 3.04e-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: 40.81  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   111 KINELQNEVSELQVKLAELlkenkslkrlqyrqEKALN----KFEDAENEISQL---IFRHNNEITALKERLRKSQEKER 183
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAEL--------------EKALAelrkELEELEEELEQLrkeLEELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   184 ATEKRVKDTESELFRTKFSLQKLKEISE------ARHLPERDDLAKKLVSAELKLDDTERRIKELSK----------NLE 247
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEeaeeelAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneeaaNLR 823

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 530383030   248 LSTNSFQRQLLAERKRAYEAHDENKVLQKEVQRLYHKLKEKERELD 293
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 112-302 3.14e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.87  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   112 INELQNEVSELQVKLAELLKENKSLK-RLQYRQEKALNKFEDaenEISQLIFRHNNEITALKERLRKSQEKERATEKRVK 190
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKsESQNKIELLLQQHQD---RIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   191 DTEsELFRTKFSLQklkeiseARHLPERDDLAKKLVSAELKLDDT-ERRIKELSKNLELSTNsfqrQLLAERKRAYEAHD 269
Cdd:pfam15921  303 IIQ-EQARNQNSMY-------MRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANS----ELTEARTERDQFSQ 370

                          170       180       190
                   ....*....|....*....|....*....|...
gi 530383030   270 ENKVLQKEVQRLYHKLKEKERELDIKNIYSNRL 302
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 91-267 3.63e-03

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: 40.82  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030    91 EPLRKDTDLVTKRILSARLlKINELQNEVSELQVKLAELLKENKSLKRlqyRQEKALNKFEDAENEISQLIFR------- 163
Cdd:TIGR02169  346 EEERKRRDKLTEEYAELKE-ELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEElqrlsee 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030   164 ---HNNEITALKERLRKSQekERATEKRVKDTESElfrtkfslQKLKEISEarhlpERDDLAKKLVSAELKLDDTERRIK 240
Cdd:TIGR02169  422 ladLNAAIAGIEAKINELE--EEKEDKALEIKKQE--------WKLEQLAA-----DLSKYEQELYDLKEEYDRVEKELS 486

                          170       180
                   ....*....|....*....|....*..
gi 530383030   241 ELSKnlELSTNSFQRQLLAERKRAYEA 267
Cdd:TIGR02169  487 KLQR--ELAEAEAQARASEERVRGGRA 511
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
119-320 4.66e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 4.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 119 VSELQVKLAELLKENKSLKRLQyrqekaLNKFEDAENEISQLiFRHNNEITALKERLRKSQEKERATEKRVKDTESELFR 198
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELN------LKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEK 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 199 TKFSLQKLKEISEARHLPER----DDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQL----LAERKRAYEAHDE 270
Cdd:COG4717  121 LEKLLQLLPLYQELEALEAElaelPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEE 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530383030 271 NKVLQKEVQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKNAA 320
Cdd:COG4717  201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 144-292 4.70e-03

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: 38.73  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  144 EKALNKFEDAENEIsqlifRHNN--EITALKERLRKSQEKERATEKRVKDTESELFRTKFSLQKLKEISEA--RHLPERD 219
Cdd:pfam13851   7 EKAFNEIKNYYNDI-----TRNNleLIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  220 DLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQrQLLAERKRAYE-----AHD-------ENKVLQKEVQRLYHKLKE 287
Cdd:pfam13851  82 KDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFE-KVERERDELYDkfeaaIQDvqqktglKNLLLEKKLQALGETLEK 160


                  ....*
gi 530383030  288 KEREL 292
Cdd:pfam13851 161 KEAQL 165
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
112-244 6.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030 112 INELQNEVSELQVKLAELlKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKER---ATEKR 188
Cdd:PRK03918 268 IEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErleELKKK 346

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530383030 189 VKDTESELFRTKFSLQKLKEISEArhLPERDDLAKKLvsAELKLDDTERRIKELSK 244
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAK--KEELERLKKRL--TGLTPEKLEKELEELEK 398
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 96-223 7.37e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 38.94  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383030  96 DTDLVTKRILSA----------RLLKINELQNEVSELQVKLAELLKENKSLKRlqyRQEKALNKFEDAENEISQLifrhN 165
Cdd:COG4026  104 DVELVRKEIKNAiiraglkslqNIPEYNELREELLELKEKIDEIAKEKEKLTK---ENEELESELEELREEYKKL----R 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530383030 166 NEITALKERLRKSQEKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAK 223
Cdd:COG4026  177 EENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEVFSLEELWKELFPEELPEEDFIYF 234
 
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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