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Conserved domains on  [gi|1953291227|ref|XP_038541775|]
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protein RUFY3 isoform X6 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
 86-241 1.09e-99

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


:

Pssm-ID: 439058  Cd Length: 156  Bit Score: 298.83  E-value: 1.09e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291227 166 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 241
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-520 4.70e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 4.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 274 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDR 353
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 354 TSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 433
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 434 DlgvKQKSELNSRLEEKTNQMAAtIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELELKQ 513
Cdd:COG1196   392 L---RAAAELAAQLEELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                  ....*..
gi 1953291227 514 ERERRLQ 520
Cdd:COG1196   468 LLEEAAL 474
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
 86-241 1.09e-99

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 298.83  E-value: 1.09e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291227 166 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 241
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 121-244 2.42e-44

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 153.58  E-value: 2.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 121 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 191
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953291227 192 KKLSEYMKALINKKELLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 244
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN smart00593
domain involved in Ras-like GTPase signaling;
181-243 5.00e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 78.04  E-value: 5.00e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291227  181 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 243
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-520 4.70e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 4.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 274 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDR 353
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 354 TSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 433
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 434 DlgvKQKSELNSRLEEKTNQMAAtIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELELKQ 513
Cdd:COG1196   392 L---RAAAELAAQLEELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                  ....*..
gi 1953291227 514 ERERRLQ 520
Cdd:COG1196   468 LLEEAAL 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 261-523 2.00e-08

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: 57.37  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  261 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 337
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  338 SSyILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 417
Cdd:TIGR02168  735 LA-RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  418 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 497
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889

                          250       260
                   ....*....|....*....|....*.
gi 1953291227  498 EELTRQRHQLELELKQERERRLQNNR 523
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRR 915
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 292-484 1.59e-05

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 47.83  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 292 LNATVNNLQAKVDALEK-SNTKLTEELAVANNRIITLQEEMERVK----EESSYILESNRKGPKQDRTSEGQALSEARKh 366
Cdd:pfam09731 263 LVSIFPDIIPVLKEDNLlSNDDLNSLIAHAHREIDQLSKKLAELKkreeKHIERALEKQKEELDKLAEELSARLEEVRA- 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 367 lKEETQLRLDVEKEL-EIQISMRQEMELAMKMLEKDVCEK-QDALVSLRQQLDdlRALKHELAFKLQssdlgvkqkSELN 444
Cdd:pfam09731 342 -ADEAQLRLEFEREReEIRESYEEKLRTELERQAEAHEEHlKDVLVEQEIELQ--REFLQDIKEKVE---------EERA 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953291227 445 SRLeEKTNQMAATIKQLEqrlrQAERGRQSAELDNRLFKQ 484
Cdd:pfam09731 410 GRL-LKLNELLANLKGLE----KATSSHSEVEDENRKAQQ 444
PRK11281 PRK11281
mechanosensitive channel MscK;
285-507 2.32e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.60  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  285 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVKEESSY----------ILESNRKGPKQDRT 354
Cdd:PRK11281   123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRP 191

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  355 SE------GQALSEA-----RKHLKEETQL------RLDvEKELEIQismRQEMELA----------MKMLEKDVCEKQD 407
Cdd:PRK11281   192 SQrvllqaEQALLNAqndlqRKSLEGNTQLqdllqkQRD-YLTARIQ---RLEHQLQllqeainskrLTLSEKTVQEAQS 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  408 ALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRleektNQMAATIKQLEQRLRQAERG--------RQSAELDN 479
Cdd:PRK11281   268 QDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTL-----TQQNLRVKNWLDRLTQSERNikeqisvlKGSLLLSR 340

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1953291227  480 RLFKQ-----------DFGDKINSLQLEVEELTRQRHQL 507
Cdd:PRK11281   341 ILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
 86-241 1.09e-99

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 298.83  E-value: 1.09e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291227 166 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 241
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 86-241 2.13e-96

RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.


Pssm-ID: 439057  Cd Length: 156  Bit Score: 290.73  E-value: 2.13e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291227 166 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 241
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
 86-240 1.14e-92

RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439043  Cd Length: 155  Bit Score: 281.00  E-value: 1.14e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17681     1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953291227 166 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 240
Cdd:cd17681    81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 86-241 5.66e-91

RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439056  Cd Length: 156  Bit Score: 276.40  E-value: 5.66e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17694     1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291227 166 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 241
Cdd:cd17694    81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 121-244 2.42e-44

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 153.58  E-value: 2.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 121 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 191
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953291227 192 KKLSEYMKALINKKELLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 244
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
 89-240 8.90e-36

RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.


Pssm-ID: 439046  Cd Length: 150  Bit Score: 130.98  E-value: 8.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  89 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLG--QNKSFWGPLELVEKLVPEAAeiTA 166
Cdd:cd17684     1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IA 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291227 167 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 240
Cdd:cd17684    77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
 97-240 1.22e-31

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


Pssm-ID: 439038  Cd Length: 154  Bit Score: 119.84  E-value: 1.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  97 SIKGLIESALNLGR-------TLDSDYAPLQQFFVVMEHCLKHGLKAKKtFLGQNKSFWGPLELVEKLVPEAAEITA--S 167
Cdd:cd17671     2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKQAirD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291227 168 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANF 240
Cdd:cd17671    81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
 89-241 1.54e-26

RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.


Pssm-ID: 439062  Cd Length: 151  Bit Score: 105.44  E-value: 1.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  89 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQN--KSFWGPLELVEKLVPEAAeiTA 166
Cdd:cd17700     1 NLITVCRFSVKTLIDRSCF--ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHNC--IC 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953291227 167 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 241
Cdd:cd17700    77 SIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
 89-241 6.34e-24

RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.


Pssm-ID: 439061  Cd Length: 151  Bit Score: 98.17  E-value: 6.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  89 NLMNMAKLSIKGLIESALnlGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQnKSFWGPLELVEKLVPEaaEIT 165
Cdd:cd17699     1 NLITVCRFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVPN--NCI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291227 166 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 241
Cdd:cd17699    76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
RUN smart00593
domain involved in Ras-like GTPase signaling;
181-243 5.00e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 78.04  E-value: 5.00e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291227  181 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 243
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
 98-237 6.32e-16

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439044  Cd Length: 150  Bit Score: 74.95  E-value: 6.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  98 IKGLIESALNLGRTLDSDYAP-LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLE-LVEKLVPEA---AEITASVKDLP 172
Cdd:cd17682     2 LKGCVLDLKSEFGEITDPDNPyLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291227 173 GLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEE-GAIIAGLLVGLNVID 237
Cdd:cd17682    82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEIlSEILLSLLYQLNEIN 147
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 87-233 1.87e-13

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.


Pssm-ID: 439041 [Multi-domain]  Cd Length: 171  Bit Score: 68.39  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  87 RMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAK-----KTFLGQN------KSFWGPLELV- 154
Cdd:cd17679     1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKfiskvSSVFSGDvdklpePNFWPLLLKFs 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 155 EKlvpeaaEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGL 233
Cdd:cd17679    81 HR------DVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGL 154
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
 171-236 3.82e-12

RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29.


Pssm-ID: 439051  Cd Length: 166  Bit Score: 64.56  E-value: 3.82e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291227 171 LPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVI 236
Cdd:cd17689    93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
 126-236 2.45e-11

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4.


Pssm-ID: 439059  Cd Length: 150  Bit Score: 61.74  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 126 MEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKK 205
Cdd:cd17697    35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1953291227 206 ELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVI 236
Cdd:cd17697   115 ELTGEWYYARSpFLSPELRSDILDSLYELNGV 146
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
 127-237 3.25e-10

RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. SGSM2, also called RUN and TBC1 domain-containing protein 1 (RUTBC1), is a GTPase-activating protein for Rab32/38, and regulates melanogenic enzyme trafficking in melanocytes. It also acts as a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins. This model contains the RUN domain of SGSM1 and SGSM2.


Pssm-ID: 439049  Cd Length: 161  Bit Score: 58.84  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 127 EHCLKHGLKAKK-TFLGQNKSFwGPLELVEKLVPEAAEITASVKDL------PGLKTPVGRGRA-------------WLR 186
Cdd:cd17687    31 DACLLHGLRKRAlGLFRSSSTF-SLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIR 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953291227 187 LALMQKKLSEYMKALINKKellSEFYEPNALMME-EEGAIIAGLLVGLNVID 237
Cdd:cd17687   110 IALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 97-218 5.11e-10

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


Pssm-ID: 439042  Cd Length: 145  Bit Score: 58.02  E-value: 5.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  97 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKktflgqNKSFWGpleLVEKLVPEAAEItaSVKDLPGLKT 176
Cdd:cd17680    12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRG------NRGYWP---FVKEFTHKETIK--QIENLPNVTT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953291227 177 PVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALM 218
Cdd:cd17680    81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 92-240 2.46e-09

RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and Phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. This model represents the RUN domain of FYCO1.


Pssm-ID: 439060  Cd Length: 158  Bit Score: 56.24  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  92 NMAKLSIKGLIESALNLGRTLDSDYAP-------LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEI 164
Cdd:cd17698     2 SQLQKIIRDLQDCVTELKKEFEETGEPitddsttLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLNDG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291227 165 TASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEP-NALMMEEEGAIIAGLLVGLNviDANF 240
Cdd:cd17698    82 IRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPrSVFLNHKYSSDIINSLYDLN--EVQF 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-520 4.70e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 4.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 274 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDR 353
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 354 TSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 433
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 434 DlgvKQKSELNSRLEEKTNQMAAtIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELELKQ 513
Cdd:COG1196   392 L---RAAAELAAQLEELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                  ....*..
gi 1953291227 514 ERERRLQ 520
Cdd:COG1196   468 LLEEAAL 474
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
 119-239 4.91e-09

RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (RUBCN) and similar proteins; RUBCN, also called rubicon, or beclin-1 associated RUN domain containing protein (Baron), is part of a Beclin-1-Vps34-containing autophagy complex. It negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. It is also an important negative regulator of the innate immune response, enhances viral replication and may play a role in viral immune evasion. This model contains the RUN domain of RUBCN.


Pssm-ID: 439048  Cd Length: 151  Bit Score: 55.35  E-value: 4.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 119 LQQFFVVMEHCLKHGLKAKKTFLGQNkSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVG-RGRAWLRLALMQKKLSEY 197
Cdd:cd17686    21 LQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGRLWLRQSLQQHCLSSQ 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953291227 198 MKALINKKELLSEFYEPNALMMEEEGAiiAGLLVGLNVIDAN 239
Cdd:cd17686   100 LQWLVSDKELLRKYYEDEAFLRQEGYA--TALLICLTAVELN 139
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
 132-241 1.48e-08

RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the first RUN domain of DENND5.


Pssm-ID: 439039  Cd Length: 183  Bit Score: 54.71  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 132 HGLKAKktflgQNKS-FWGPL----ELVEKLVPEAAEITA---SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALIN 203
Cdd:cd17677    65 HGLQTK-----QGKSaLWSHLlayqENEERLKPLPESLLFdmkNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1953291227 204 KKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 241
Cdd:cd17677   140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVDY-FC 177
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 261-523 2.00e-08

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: 57.37  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  261 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 337
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  338 SSyILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 417
Cdd:TIGR02168  735 LA-RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  418 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 497
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889

                          250       260
                   ....*....|....*....|....*.
gi 1953291227  498 EELTRQRHQLELELKQERERRLQNNR 523
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRR 915
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
 168-241 1.78e-07

RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B.


Pssm-ID: 439053 [Multi-domain]  Cd Length: 206  Bit Score: 51.98  E-value: 1.78e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953291227 168 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 241
Cdd:cd17691   127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVDY-FC 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-524 9.08e-07

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: 51.98  E-value: 9.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  272 DGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERV---KEESSYILESNRK- 347
Cdd:TIGR02168  266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELAEELAELEEk 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  348 --GPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHE 425
Cdd:TIGR02168  346 leELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  426 LAFKLQSsdlgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFkQDFGDKINSLQLEVEELtrQRH 505
Cdd:TIGR02168  426 LLKKLEE-----AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSL--ERL 497

                          250
                   ....*....|....*....
gi 1953291227  506 QLELELKQERERRLQNNRS 524
Cdd:TIGR02168  498 QENLEGFSEGVKALLKNQS 516
RUN_SGSM1 cd17703
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ...
 98-232 2.26e-06

RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. This model contains the RUN domain of SGSM1.


Pssm-ID: 439065  Cd Length: 177  Bit Score: 48.08  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  98 IKGLIESALNLgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKT-FLGQNK----------SFWGPLELVEKL--------- 157
Cdd:cd17703     3 VKQIMEEAVTR-KFVHEDSSHIISFCAAVEACVLHGLKRRAAgFLRSNKiaalfmkvgkSFPPAEELCRKVqeleqllen 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 158 ----VPEAAEITASVKDLPGLkTPVGRGRAWLRLALMQKKLSEYMKALInkkELLSEFYEPNALMMEE-EGAIIAGLLVG 232
Cdd:cd17703    82 krnqMQGLQENVRKMPKLPNL-SPQAIKHLWIRTALFEKVLDKIVHYLV---ENSSKYYEKEALLMDPvDGPILASLLVG 157
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-516 2.81e-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: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 276 TAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQD 352
Cdd:COG1196   267 AELEELRLELEELELELEeaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE-ELEEELEELEEE 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 353 RTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS 432
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 433 SDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQdfgdKINSLQLEVEELtRQRHQLELELK 512
Cdd:COG1196   426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA----ALAELLEELAEA-AARLLLLLEAE 500


                  ....
gi 1953291227 513 QERE 516
Cdd:COG1196   501 ADYE 504
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 360-520 2.85e-06

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 50.34  E-value: 2.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  360 LSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDV--CEKQDALVSLRQQLDDLRALKHelafklqssdlgv 437
Cdd:COG3096    443 LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWQTARELLRRYRSQQA------------- 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  438 kqkselnsrLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINsLQLEVEELTRQRHQLELELKQERER 517
Cdd:COG3096    510 ---------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEAQLEELEEQAAEAVEQ 579


                   ...
gi 1953291227  518 RLQ 520
Cdd:COG3096    580 RSE 582
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-476 5.44e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 274 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnRKGPKQDR 353
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--------LAEAEEAL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 354 TSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 433
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953291227 434 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAE 476
Cdd:COG1196   448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 269-518 5.62e-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: 49.67  E-value: 5.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  269 SEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnRKG 348
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  349 PKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 428
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  429 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRqaERGRQSAELDNRLfKQDFGDKINSLQLEVEELTRQRHQL- 507
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-ENKIEDDEEEARRRLKRLENKIKELg 985

                          250
                   ....*....|....*..
gi 1953291227  508 ------ELELKQERERR 518
Cdd:TIGR02168  986 pvnlaaIEEYEELKERY 1002
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 327-518 6.16e-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: 6.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  327 LQEEMERVKEESsYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQ 406
Cdd:TIGR02169  672 EPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  407 DALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ 467
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLTLEKEY 830

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953291227  468 AERGRQSAELDNRLFK---QDFGDKINSLQLEVEELTRQRHQLELELKQERERR 518
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 292-484 1.59e-05

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 47.83  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 292 LNATVNNLQAKVDALEK-SNTKLTEELAVANNRIITLQEEMERVK----EESSYILESNRKGPKQDRTSEGQALSEARKh 366
Cdd:pfam09731 263 LVSIFPDIIPVLKEDNLlSNDDLNSLIAHAHREIDQLSKKLAELKkreeKHIERALEKQKEELDKLAEELSARLEEVRA- 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 367 lKEETQLRLDVEKEL-EIQISMRQEMELAMKMLEKDVCEK-QDALVSLRQQLDdlRALKHELAFKLQssdlgvkqkSELN 444
Cdd:pfam09731 342 -ADEAQLRLEFEREReEIRESYEEKLRTELERQAEAHEEHlKDVLVEQEIELQ--REFLQDIKEKVE---------EERA 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953291227 445 SRLeEKTNQMAATIKQLEqrlrQAERGRQSAELDNRLFKQ 484
Cdd:pfam09731 410 GRL-LKLNELLANLKGLE----KATSSHSEVEDENRKAQQ 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 301-525 1.59e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 301 AKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRkgpkQDRTSEGQALSEARKHLKEETQLRLDVEKE 380
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAE----LEELR----LELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 381 LEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELafklqssdlgvkqkselnsrlEEKTNQMAATIKQ 460
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA---------------------EEELEEAEAELAE 362

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953291227 461 LEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLElELKQERERRLQNNRSI 525
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE-ALLERLERLEEELEEL 426
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
300-525 1.78e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  300 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE-SSYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVE 378
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERrEALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  379 kELEIQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQssDLGVKQKSELNSRLEEK------TN 452
Cdd:COG4913    689 -ALEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERfaaalgDA 762

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  453 QMAATIKQLEQRLRQAERGRQSAEldNRL------FKQDFGDKINSLQLEVEELT---RQRHQLE---LELKQERERRLQ 520
Cdd:COG4913    763 VERELRENLEERIDALRARLNRAE--EELeramraFNREWPAETADLDADLESLPeylALLDRLEedgLPEYEERFKELL 840


                   ....*
gi 1953291227  521 NNRSI 525
Cdd:COG4913    841 NENSI 845
PRK11281 PRK11281
mechanosensitive channel MscK;
285-507 2.32e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.60  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  285 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVKEESSY----------ILESNRKGPKQDRT 354
Cdd:PRK11281   123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRP 191

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  355 SE------GQALSEA-----RKHLKEETQL------RLDvEKELEIQismRQEMELA----------MKMLEKDVCEKQD 407
Cdd:PRK11281   192 SQrvllqaEQALLNAqndlqRKSLEGNTQLqdllqkQRD-YLTARIQ---RLEHQLQllqeainskrLTLSEKTVQEAQS 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  408 ALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRleektNQMAATIKQLEQRLRQAERG--------RQSAELDN 479
Cdd:PRK11281   268 QDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTL-----TQQNLRVKNWLDRLTQSERNikeqisvlKGSLLLSR 340

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1953291227  480 RLFKQ-----------DFGDKINSLQLEVEELTRQRHQL 507
Cdd:PRK11281   341 ILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 280-456 2.39e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 280 DQKNYVEELNRhLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE------SSY-----------IL 342
Cdd:COG3883    31 ELEAAQAELDA-LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerarALYrsggsvsyldvLL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 343 ESN------------RKGPKQDRtsegQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALV 410
Cdd:COG3883   110 GSEsfsdfldrlsalSKIADADA----DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953291227 411 SLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAA 456
Cdd:COG3883   186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 269-527 3.41e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 3.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  269 SEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEElavannRIITLQEEMERVKEESSYILESNRKG 348
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  349 PKQDRTSEGQA----------LSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQ 415
Cdd:TIGR02169  314 ERELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  416 LDDLR----ALKHELAFKLQSSDLGVKQKSELN---SRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDnrlfKQDFGD 488
Cdd:TIGR02169  394 LEKLKreinELKRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQ 469

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1953291227  489 KINSLQLEVEELTRQRHQLELELKQERERRLQNNRSIPG 527
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 273-517 5.65e-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: 5.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 273 GQITAILDQKNYVEELNRHLNAtvnnLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQD 352
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 353 RTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQE----MELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 428
Cdd:COG4942    92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 429 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERgrqsaeldnrlfkqdfgdKINSLQLEVEELTRQRHQLE 508
Cdd:COG4942   172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA------------------ELAELQQEAEELEALIARLE 233


                  ....*....
gi 1953291227 509 LELKQERER 517
Cdd:COG4942   234 AEAAAAAER 242
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 328-568 6.56e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 328 QEEMERVKEESSYILESNRKGPKQDRTSEGQALSEARKHLKEEtQLRLDVEKELE-IQIS--------MRQEmELAMKM- 397
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE-RMAMERERELErIRQEerkrelerIRQE-EIAMEIs 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 398 ----LEKDVCEKQDALVSLRQQLDDLRALK-----HELAFKLQSSDLGVKQKSELNSRL-------EEKTNQMAATIKQL 461
Cdd:pfam17380 376 rmreLERLQMERQQKNERVRQELEAARKVKileeeRQRKIQQQKVEMEQIRAEQEEARQrevrrleEERAREMERVRLEE 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 462 EQRLRQAERGRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRHQLELE------LKQERERRL-------------QNN 522
Cdd:pfam17380 456 QERQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKILEKELEerkqamIEEERKRKLlekemeerqkaiyEEE 533

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1953291227 523 RSIPGKGSQKPEPKTDGKHKIQEEnvkLKKPLDESHRDEKTEEHRE 568
Cdd:pfam17380 534 RRREAEEERRKQQEMEERRRIQEQ---MRKATEERSRLEAMERERE 576
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
297-525 8.04e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 8.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 297 NNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTSE-GQALSEARKHLkEETQLRL 375
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSElESQLAEARAEL-AEAEARL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 376 DvekELEIQISMRQEmelAMKMLEKDvcekqDALVSLRQQLDDLRAlkhelafklqssdlgvkQKSELNSRLEEKTNQMA 455
Cdd:COG3206   243 A---ALRAQLGSGPD---ALPELLQS-----PVIQQLRAQLAELEA-----------------ELAELSARYTPNHPDVI 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 456 ATIKQLE--QRLRQAERGRQSAELDNRlfkqdfgdkINSLQLEVEELTRQRHQLELELKQ---------ERERRLQNNRS 524
Cdd:COG3206   295 ALRAQIAalRAQLQQEAQRILASLEAE---------LEALQAREASLQAQLAQLEARLAElpeleaelrRLEREVEVARE 365


                  .
gi 1953291227 525 I 525
Cdd:COG3206   366 L 366
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
 168-241 1.56e-04

RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A.


Pssm-ID: 439052 [Multi-domain]  Cd Length: 209  Bit Score: 43.07  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953291227 168 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 241
Cdd:cd17690   130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVDY-FC 203
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-525 2.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 353 RTSEGQALSEARKHLKEETQLRLDVEKELEIQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS 432
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAEL---EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 433 SDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDnrlfKQDFGDKINSLQLEVEELTRQRHQLELELK 512
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         170
                  ....*....|...
gi 1953291227 513 QERERRLQNNRSI 525
Cdd:COG1196   376 EAEEELEELAEEL 388
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
295-570 3.26e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 295 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTSEgqalSEARKHLKEETQLR 374
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 375 L-DVEKELEIQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 453
Cdd:PRK03918  461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 454 MAATIKQLEQRLRQAErgrqsaELDNRLFKQDfgDKINSLQLEVEELTRQRHQLELELKQERERRLQN-----NRSIPGK 528
Cdd:PRK03918  537 LKGEIKSLKKELEKLE------ELKKKLAELE--KKLDELEEELAELLKELEELGFESVEELEERLKElepfyNEYLELK 608

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291227 529 GSQKPEPKTDGKHKIQEENV---------------KLKKPLDESHRDEKTEEHREAK 570
Cdd:PRK03918  609 DAEKELEREEKELKKLEEELdkafeelaetekrleELRKELEELEKKYSEEEYEELR 665
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 330-469 6.17e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 330 EMERVKEES---SYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQ 406
Cdd:pfam17380 447 EMERVRLEEqerQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291227 407 DALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQKSELNSRLE--EKTNQMAATIKQLEQRLRQAE 469
Cdd:pfam17380 527 KAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKATEERSRLEamEREREMMRQIVESEKARAEYE 592
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 260-519 6.96e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 260 LKDGNSSKGSEGDGQITAILDQKNYVEELNRHLNATvnNLQAKVDALEKSNTkltEELAVANNRIITL-------QEEME 332
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQ---EEIAMEISRMRELerlqmerQQKNE 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 333 RVKEE-----SSYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMElamkmlekdvceKQD 407
Cdd:pfam17380 393 RVRQEleaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE------------RQQ 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 408 ALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-----SELNSRLE---EKTNQMAATIKQLEQRLRQ--AERGRQSAEL 477
Cdd:pfam17380 461 QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkileKELEERKQamiEEERKRKLLEKEMEERQKAiyEEERRREAEE 540

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1953291227 478 DNRlfKQDFGDKINSLQLEVEELTRQRHQLElelKQERERRL 519
Cdd:pfam17380 541 ERR--KQQEMEERRRIQEQMRKATEERSRLE---AMEREREM 577
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 274-470 9.01e-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: 42.36  E-value: 9.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  274 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAvaNNRIITLQEEMERVKEESSYILESNR--KGPKQ 351
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLReiEQKLN 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  352 DRTSEGQALSEARKHLKEETqlrldveKELEIQISMRQ----EMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 427
Cdd:TIGR02169  823 RLTLEKEYLEKEIQELQEQR-------IDLKEQIKSIEkeieNLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1953291227  428 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAER 470
Cdd:TIGR02169  896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
mukB PRK04863
chromosome partition protein MukB;
360-526 1.75e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  360 LSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 437
Cdd:PRK04863   444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  438 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAErGRQSAELDNRLFKQDF----GDKINSLQLEVEELTRQRHQLELELK 512
Cdd:PRK04863   519 RMRlSELEQRLRQQ--------QRAERLLAEFC-KRLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589

                          170
                   ....*....|....
gi 1953291227  513 QERERRLQNNRSIP 526
Cdd:PRK04863   590 QLQARIQRLAARAP 603
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
358-518 1.90e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 358 QALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVcEKQDALVSLRQQLDDLRALKHELAfklqssdlgv 437
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-EKLEKLLQLLPLYQELEALEAELA---------- 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 438 kqksELNSRLEEKTNQMAA---TIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELELKQE 514
Cdd:COG4717   143 ----ELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218


                  ....
gi 1953291227 515 RERR 518
Cdd:COG4717   219 QEEL 222
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 368-520 2.77e-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: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 368 KEETQLRL-----------DVEKELEIQI-SMRQEMELAMKML----EKDVCEKQDALVSLRQQLDDLRALKHELAFKLQ 431
Cdd:COG1196   174 KEEAERKLeateenlerleDILGELERQLePLERQAEKAERYRelkeELKELEAELLLLKLRELEAELEELEAELEELEA 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 432 SSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRL-RQAERGRQSAELDNRLFKQDfgDKINSLQLEVEELTRQRHQLELE 510
Cdd:COG1196   254 ELEELEAELAELEAELEELRLELEELELELEEAQaEEYELLAELARLEQDIARLE--ERRRELEERLEELEEELAELEEE 331

                         170
                  ....*....|
gi 1953291227 511 LKQERERRLQ 520
Cdd:COG1196   332 LEELEEELEE 341
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 287-570 3.31e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 287 ELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI----------LESNRKGPKQDRTSE 356
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAkaahsfvvteFEATTCSLEELLRTE 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 357 GQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQ---QLDDLRALKHELAFKLQSS 433
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekIAEELKGKEQELIFLLQAR 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 434 DlgvKQKSELNSRLEEKTNQMAATIKQLEQrlrqaergrQSAELDNRLFKQ-DFGDKINSLQLEVEELTRQRHQLELELK 512
Cdd:pfam05483 449 E---KEIHDLEIQLTAIKTSEEHYLKEVED---------LKTELEKEKLKNiELTAHCDKLLLENKELTQEASDMTLELK 516

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953291227 513 QERERRLQNNRsipgkgsqKPEPKTDGKHKIQEENVKLKKPLdESHRDEKTEEHREAK 570
Cdd:pfam05483 517 KHQEDIINCKK--------QEERMLKQIENLEEKEMNLRDEL-ESVREEFIQKGDEVK 565
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 286-516 4.64e-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: 40.16  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  286 EELNRHLNATVNNLQAKVDALEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYILESNRKGPKQDRTSEgQALS 361
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLDEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  362 EARKHLKEE-------TQLRL-------DVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 427
Cdd:pfam01576  163 EFTSNLAEEeekakslSKLKNkheamisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  428 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVEE-LTRQRHQ 506
Cdd:pfam01576  243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALKTELEDtLDTTAAQ 318

                          250
                   ....*....|
gi 1953291227  507 LELELKQERE 516
Cdd:pfam01576  319 QELRSKREQE 328
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
274-464 5.43e-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: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  274 QITAILDQKNYVEELNRHLNAtvnnlQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRkgpKQDR 353
Cdd:COG4913    266 AARERLAELEYLRAALRLWFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREE----LDELE---AQIR 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  354 TSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSs 433
Cdd:COG4913    334 GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA- 412

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1953291227  434 dlgvkQKSELNSRLEEKTNQmaatIKQLEQR 464
Cdd:COG4913    413 -----ALRDLRRELRELEAE----IASLERR 434
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 288-468 5.91e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.65  E-value: 5.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  288 LNRHLNATVNNLQAKVDALEK--SNTKLTEELAVANNRII----TLQEEMERVKEessyILESNRKGPKQdRTSEGQALS 361
Cdd:PRK10929    80 LSAELRQQLNNERDEPRSVPPnmSTDALEQEILQVSSQLLeksrQAQQEQDRARE----ISDSLSQLPQQ-QTEARRQLN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227  362 EARKHLK-------------------EETQLRLDVEkELEI-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDD 418
Cdd:PRK10929   155 EIERRLQtlgtpntplaqaqltalqaESAALKALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNS 233

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953291227  419 LRALKHELAFKL------QSSDL--GVKQKSELNSRLEEKTNQMAATIKQLEQRLRQA 468
Cdd:PRK10929   234 QRQREAERALEStellaeQSGDLpkSIVAQFKINRELSQALNQQAQRMDLIASQQRQA 291
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 351-524 6.66e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 351 QDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL 430
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 431 Q------SSDLGVKQKSELNSRLEEKTNQ--------MAATIKQL-EQRLRQAERGRQSAELDNRLfKQDFGDKINSLQL 495
Cdd:COG4942   100 EaqkeelAELLRALYRLGRQPPLALLLSPedfldavrRLQYLKYLaPARREQAEELRADLAELAAL-RAELEAERAELEA 178

                         170       180
                  ....*....|....*....|....*....
gi 1953291227 496 EVEELTRQRHQLElELKQERERRLQNNRS 524
Cdd:COG4942   179 LLAELEEERAALE-ALKAERQKLLARLEK 206
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 295-462 7.12e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.59  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 295 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRkgpkqdrtsegQALSEARKHLKEETQLR 374
Cdd:pfam09787  41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSR-----------EQLQELEEQLATERSAR 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 375 LDVEKELEiqiSMRQEMElamKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSdlgvKQKSELNSRLEEKTNQM 454
Cdd:pfam09787 110 REAEAELE---RLQEELR---YLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSS----SSQSELENRLHQLTETL 179


                  ....*...
gi 1953291227 455 AATIKQLE 462
Cdd:pfam09787 180 IQKQTMLE 187
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 296-520 8.30e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 38.96  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 296 VNNLQAKVDALEKSNTKL-------TEELAVANNRIITLQEEMERVKEE---SSYILESNRKG---------PKQDRTSE 356
Cdd:pfam07111 164 LSSLTSKAEGLEKSLNSLetkrageAKQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYvgeqvppevHSQTWELE 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 357 GQALSEARKHLKEEtqlRLDVEKELEI-QISMR--------QEMELAMKMLEKDVCEKQDALvSLRQQLDDLRALKHELA 427
Cdd:pfam07111 244 RQELLDTMQHLQED---RADLQATVELlQVRVQslthmlalQEEELTRKIQPSDSLEPEFPK-KCRSLLNRWREKVFALM 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 428 FKLQSSDLgvkqkselnsrleektnQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKinSLQLEVEELTRQRHQL 507
Cdd:pfam07111 320 VQLKAQDL-----------------EHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDK--AAEVEVERMSAKGLQM 380

                         250
                  ....*....|...
gi 1953291227 508 ELELKQERERRLQ 520
Cdd:pfam07111 381 ELSRAQEARRRQQ 393
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 389-517 9.98e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 9.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291227 389 QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDlgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQA 468
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKLQAEIAEAEAEIEERREELGERARAL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953291227 469 ERGRQSAELDNRLFK-QDFGDKINSLQLeVEELTRQRHQLELELKQERER 517
Cdd:COG3883    96 YRSGGSVSYLDVLLGsESFSDFLDRLSA-LSKIADADADLLEELKADKAE 144
 
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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