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Conserved domains on  [gi|847088409|ref|XP_012820410|]
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protein RUFY3 isoform X7 [Xenopus tropicalis]

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 1.07e-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: 296.14  E-value: 1.07e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409 166 ASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIISGLLVGLNVIDANFC 241
Cdd:cd17696   81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-482 4.96e-09

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 4.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   272 DGQITAILDQKNYVEELNRQLSATVNNLQAKVDALEKSNTKLTEELAVA-------NNRIITMQEEMERIKEETSYYSEA 344
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqkelyalANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   345 SKKVN------KQERTADGQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDD 418
Cdd:TIGR02168  318 LEELEaqleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409   419 LRALKHELSFKLQSSDLALKQKSELNSRLEEK--TNQMAATVKQLEQSEKDLVKQAKTLNSVAHKL 482
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEAL 463
 
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 1.07e-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: 296.14  E-value: 1.07e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409 166 ASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIISGLLVGLNVIDANFC 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 5.24e-45

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: 153.97  E-value: 5.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  121 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLRT---PVGRGRAWLRLALMQ 191
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 847088409  192 KKLSEYMKALINRKDLLSEFYEPNALMMEEEGA-IISGLLVGLNVIDANFCMKG 244
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN smart00593
domain involved in Ras-like GTPase signaling;
181-243 4.08e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 75.34  E-value: 4.08e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847088409   181 GRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIISGLLVGLNVIDANFCMK 243
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-482 4.96e-09

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: 58.91  E-value: 4.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   272 DGQITAILDQKNYVEELNRQLSATVNNLQAKVDALEKSNTKLTEELAVA-------NNRIITMQEEMERIKEETSYYSEA 344
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqkelyalANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   345 SKKVN------KQERTADGQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDD 418
Cdd:TIGR02168  318 LEELEaqleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409   419 LRALKHELSFKLQSSDLALKQKSELNSRLEEK--TNQMAATVKQLEQSEKDLVKQAKTLNSVAHKL 482
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEAL 463
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 273-482 2.67e-08

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: 55.93  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 273 GQITAILDQKNYVEELNRQLSAtvnnLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEETSYYSEASKKVNKQE 352
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 353 RTADGQaLSEVKKHLKEETQLRLDIEKELEVQIGMRQE----MELAMKMLDKDVCEKQDALAALRQQLDDLRALKHELSF 428
Cdd:COG4942   93 AELRAE-LEAQKEELAELLRALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 847088409 429 KLQSSDLALKQKSELNSRLEEKTNQMAATVKQLEQSEKDLVKQAKTLNSVAHKL 482
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 281-468 5.57e-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: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  281 QKNyvEELNRQLSATvnnlqAKVDALEKSNTKLTEELAVANNRIITMQE----------------EMERIKEETSYYSEA 344
Cdd:pfam17380 389 QKN--ERVRQELEAA-----RKVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEQERQQQ 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  345 SKKVNKQERTADGQALS---EVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALA--ALRQQLDDL 419
Cdd:pfam17380 462 VERLRQQEEERKRKKLElekEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEE 541

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 847088409  420 RALKHELSFKLQSSDlALKQKSELNSRLE--EKTNQMAATVKQLEQSEKDL 468
Cdd:pfam17380 542 RRKQQEMEERRRIQE-QMRKATEERSRLEamEREREMMRQIVESEKARAEY 591
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 327-442 2.77e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 39.23  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 327 MQEEM-----ERIKEETSYYSEASKKVNK----QERTADGQALSEVKKHLKEETQLRLDIEKELEVQI-----GMRQEME 392
Cdd:cd07649   20 MQKEMaefirERIKIEEEYAKNLSKLSQSslaaQEEGTLGEAWAQVKKSLADEAEVHLKFSSKLQSEVekpllNFRENFK 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 847088409 393 LAMKMLDKDVCE--KQDAL--AALRQQLDDLRALKHELSFKLQSSDLALKQKSE 442
Cdd:cd07649  100 KDMKKLDHHIADlrKQLASryAAVEKARKALLERQKDLEGKTQQLEIKLSNKTE 153
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
295-482 4.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 295 TVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEETSYYSEASKK--VNKQERTadgqalSEVKKHLKEETQ 372
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELT------EEHRKELLEEYT 458

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 373 LRL-DIEKELEVQIGMRQEMELAMKMLDKdVCEKQDALAALRQQLDDLRALKHELS-FKLQSsdlaLKQKSELNSRLEEK 450
Cdd:PRK03918 459 AELkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKkYNLEE----LEKKAEEYEKLKEK 533

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 847088409 451 TNQMAATVKQLE---QSEKDLVKQAKTLNSVAHKL 482
Cdd:PRK03918 534 LIKLKGEIKSLKkelEKLEELKKKLAELEKKLDEL 568
 
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 1.07e-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: 296.14  E-value: 1.07e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409 166 ASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIISGLLVGLNVIDANFC 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 3.19e-98

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: 292.27  E-value: 3.19e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17695    1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409 166 ASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIISGLLVGLNVIDANFC 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 4.00e-95

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: 284.46  E-value: 4.00e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17681    1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847088409 166 ASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIISGLLVGLNVIDANF 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 1.40e-92

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: 277.94  E-value: 1.40e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17694    1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409 166 ASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIISGLLVGLNVIDANFC 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 5.24e-45

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: 153.97  E-value: 5.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  121 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLRT---PVGRGRAWLRLALMQ 191
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 847088409  192 KKLSEYMKALINRKDLLSEFYEPNALMMEEEGA-IISGLLVGLNVIDANFCMKG 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 9.34e-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: 129.83  E-value: 9.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  89 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLG--QNKSFWGPLELVEKLVPEAAeiTA 166
Cdd:cd17684    1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847088409 167 SVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIISGLLVGLNVIDANF 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 3.81e-32

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: 120.22  E-value: 3.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  97 SIKGLIESALNLGR-------TLDSDYAPLQQFFVVMEHCLKHGLKAKKtFLGQNKSFWGPLELVEKLVPEAAEITA--S 167
Cdd:cd17671    2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKQAirD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847088409 168 VKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIISGLLVGLNVIDANF 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 3.61e-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: 103.90  E-value: 3.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  89 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQN--KSFWGPLELVEKLVPEAAeiTA 166
Cdd:cd17700    1 NLITVCRFSVKTLIDRSCF--ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHNC--IC 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847088409 167 SVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIISGLLVGLNVIDANFC 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 6.92e-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: 97.40  E-value: 6.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  89 NLMNMAKLSIKGLIESALnlGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQnKSFWGPLELVEKLVPEaaEIT 165
Cdd:cd17699    1 NLITVCRFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVPN--NCI 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409 166 ASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIISGLLVGLNVIDANFC 241
Cdd:cd17699   76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
RUN smart00593
domain involved in Ras-like GTPase signaling;
181-243 4.08e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 75.34  E-value: 4.08e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847088409   181 GRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIISGLLVGLNVIDANFCMK 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 6.50e-17

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: 77.65  E-value: 6.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  98 IKGLIESALNLGRTLDSDYAP-LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLE-LVEKLVPEA---AEITASVKDLP 172
Cdd:cd17682    2 LKGCVLDLKSEFGEITDPDNPyLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409 173 GLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEE-GAIISGLLVGLNVID 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 1.66e-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: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  87 RMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAK-----KTFLGQN------KSFWGPLELV- 154
Cdd:cd17679    1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKfiskvSSVFSGDvdklpePNFWPLLLKFs 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 155 EKlvpeaaEITASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIISGLLVGL 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 2.83e-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: 64.94  E-value: 2.83e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 847088409 171 LPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIISGLLVGLNVI 236
Cdd:cd17689   93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 97-218 8.10e-11

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: 59.95  E-value: 8.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  97 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKktflgqNKSFWGpleLVEKLVPEAAEItaSVKDLPGLRT 176
Cdd:cd17680   12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRG------NRGYWP---FVKEFTHKETIK--QIENLPNVTT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 847088409 177 PVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALM 218
Cdd:cd17680   81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
 126-236 1.92e-10

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: 59.04  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 126 MEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRK 205
Cdd:cd17697   35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114

                         90       100       110
                 ....*....|....*....|....*....|..
gi 847088409 206 DLLSEFYEPNA-LMMEEEGAIISGLLVGLNVI 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 2.82e-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: 2.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 127 EHCLKHGLKAKK-TFLGQNKSFwGPLELVEKLVPEAAEITASVKDL------PGLRTPVGRGRA-------------WLR 186
Cdd:cd17687   31 DACLLHGLRKRAlGLFRSSSTF-SLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIR 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 847088409 187 LALMQKKLSEYMKALINRKdllSEFYEPNALMME-EEGAIISGLLVGLNVID 237
Cdd:cd17687  110 IALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 92-240 2.45e-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: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  92 NMAKLSIKGLIESALNLGRTLDSDYAP-------LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEI 164
Cdd:cd17698    2 SQLQKIIRDLQDCVTELKKEFEETGEPitddsttLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLNDG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 847088409 165 TASVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEP-NALMMEEEGAIISGLLVGLNviDANF 240
Cdd:cd17698   82 IRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPrSVFLNHKYSSDIINSLYDLN--EVQF 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-482 4.96e-09

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: 58.91  E-value: 4.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   272 DGQITAILDQKNYVEELNRQLSATVNNLQAKVDALEKSNTKLTEELAVA-------NNRIITMQEEMERIKEETSYYSEA 344
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqkelyalANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   345 SKKVN------KQERTADGQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDD 418
Cdd:TIGR02168  318 LEELEaqleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847088409   419 LRALKHELSFKLQSSDLALKQKSELNSRLEEK--TNQMAATVKQLEQSEKDLVKQAKTLNSVAHKL 482
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEAL 463
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
 106-239 7.70e-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: 54.58  E-value: 7.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 106 LNLGRTLD--SDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNkSFWGPLELVEKLVPEAAEITASVKDLPGLRTPVG-RGR 182
Cdd:cd17686    6 LLLSRSSNvwSTYGGLQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGR 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 847088409 183 AWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAiiSGLLVGLNVIDAN 239
Cdd:cd17686   85 LWLRQSLQQHCLSSQLQWLVSDKELLRKYYEDEAFLRQEGYA--TALLICLTAVELN 139
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
 132-241 1.94e-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: 53.94  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 132 HGLKAKktflgQNKS-FWGPL----ELVEKLVPEAAEITA---SVKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALIN 203
Cdd:cd17677   65 HGLQTK-----QGKSaLWSHLlayqENEERLKPLPESLLFdmkNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 847088409 204 RKDLLSEFYEPNA-LMMEEEGAIISGLLVGLNVIDAnFC 241
Cdd:cd17677  140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVDY-FC 177
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 273-482 2.67e-08

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: 55.93  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 273 GQITAILDQKNYVEELNRQLSAtvnnLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEETSYYSEASKKVNKQE 352
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 353 RTADGQaLSEVKKHLKEETQLRLDIEKELEVQIGMRQE----MELAMKMLDKDVCEKQDALAALRQQLDDLRALKHELSF 428
Cdd:COG4942   93 AELRAE-LEAQKEELAELLRALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 847088409 429 KLQSSDLALKQKSELNSRLEEKTNQMAATVKQLEQSEKDLVKQAKTLNSVAHKL 482
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-486 3.10e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 3.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 290 RQLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEETSYYSEASKKVNKQERTADgQALSEVKKHLKE 369
Cdd:COG1196  263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-EELEELEEELEE 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 370 ETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALKHELSFKLQSSDLALKQKSELNSRLEE 449
Cdd:COG1196  342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 847088409 450 KTNQMAATVKQLEQSEKDLVKQAKTLNSVAHKLLQKQ 486
Cdd:COG1196  422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-478 8.94e-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: 55.06  E-value: 8.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   272 DGQITAILDQKNYVEELNRQ---LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEEtsyYSEASKKV 348
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD---LARLEAEV 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   349 NKQERTADgQALSEVKKHLKEETQLRLDIEK---ELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALKHE 425
Cdd:TIGR02168  743 EQLEERIA-QLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 847088409   426 LSFKLQSS--DLALKQKS--ELNSRLEEKTNQMAATVKQLEQSEKDLVKQAKTLNSV 478
Cdd:TIGR02168  822 LRERLESLerRIAATERRleDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
 168-241 2.02e-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: 51.59  E-value: 2.02e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847088409 168 VKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNA-LMMEEEGAIISGLLVGLNVIDAnFC 241
Cdd:cd17691  127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVDY-FC 200
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 274-456 3.14e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.52  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 274 QITAILDQknyVEELNRQLSAT---VNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEM-ERIKE------ETSY--- 340
Cdd:COG3883   31 ELEAAQAE---LDALQAELEELneeYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARAlyrsggSVSYldv 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 341 ------YSEASKKVNKQER--TADGQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAAL 412
Cdd:COG3883  108 llgsesFSDFLDRLSALSKiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 847088409 413 RQQLDDLRALKHELSFKLQSSDLALKQKSELNSRLEEKTNQMAA 456
Cdd:COG3883  188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-484 6.15e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 6.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 274 QITAILDQKNYVEELNRQLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERikeetsyySEASKKVNKQER 353
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE--------AEAELAEAEEAL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 354 TADGQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALKHELSFKLQSS 433
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 847088409 434 DLALKQKSELNSRLEEKTNQMAATVKQLEQSEKDLVKQAKTLNSVAHKLLQ 484
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-486 1.95e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 290 RQLSATVNNLQAKVDALEKSNtkLTEELAVANNRIITMQEEMERIKEETSYySEASKKVNKQERTADGQALSEVKKHLKE 369
Cdd:COG1196  216 RELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 370 ETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALKHELSFKLQSSDLALKQKSELNSRLEE 449
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 847088409 450 KTNQMAATVKQLEQSEKDLVKQAKTLNSVAHKLLQKQ 486
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-486 3.11e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 274 QITAILDQKNYVEELNRQLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEETSYYsEASKKVNKQER 353
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL-EQDIARLEERR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 354 TADGQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALKHELSFKLQSs 433
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE- 390

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 847088409 434 dlALKQKSELNSRLEEKTNQMAATVKQLEQSEKDLVKQAKTLNSVAHKLLQKQ 486
Cdd:COG1196  391 --ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-486 7.75e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 7.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 276 TAILDQKNYVEELNRQLS---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEETSYYSE------ASK 346
Cdd:COG1196  267 AELEELRLELEELELELEeaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleeleEEL 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 347 KVNKQERTADGQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALKHEL 426
Cdd:COG1196  347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 427 SFKLQSSDLALKQKSELNSRLEEKTNQMAATVKQLEQSEKDLVKQAKTLNSVAHKLLQKQ 486
Cdd:COG1196  427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 269-473 1.02e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   269 SEGDGQITAILDQKNYVEELNRQLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEE----MERIKEETSYYSEA 344
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRERLESLERRIAAT 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   345 SKKVNKQERTADGQA--LSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRAL 422
Cdd:TIGR02168  837 ERRLEDLEEQIEELSedIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 847088409   423 KHELSFKLQSSDLAL---KQK-SELNSRLEEKTNQMAATVKQLEQSEKDLVKQAK 473
Cdd:TIGR02168  917 LEELREKLAQLELRLeglEVRiDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 285-486 1.51e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   285 VEELNRQLsatvNNLQAKVDALEKSNTKLTE----ELAVANNRIITMQEEMERIKEETSYYSEASKKVNKQERTADGQ-- 358
Cdd:TIGR02168  195 LNELERQL----KSLERQAEKAERYKELKAElrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKle 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   359 ----ALSEVKKHLKEETQLRLDIEKE---LEVQIGMRQEmelAMKMLDKDVCEKQDALAALRQQLDDLRALKHELSFKLQ 431
Cdd:TIGR02168  271 elrlEVSELEEEIEELQKELYALANEisrLEQQKQILRE---RLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 847088409   432 SsdlALKQKSELNSRLEEKtnqmAATVKQLEQSEKDLVKQAKTLNSVAHKLLQKQ 486
Cdd:TIGR02168  348 E---LKEELESLEAELEEL----EAELEELESRLEELEEQLETLRSKVAQLELQI 395
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 274-475 4.72e-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: 4.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 274 QITAILDQknyVEELNRQLSAtvnnLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEEtsyYSEASKKVNKQER 353
Cdd:COG4942   49 EEKALLKQ---LAALERRIAA----LARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE---LAELLRALYRLGR 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 354 TADGQALSEVKKHLKEETQLRLdiekeLEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRAlkhELSFKLQSS 433
Cdd:COG4942  119 QPPLALLLSPEDFLDAVRRLQY-----LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA---ELEEERAAL 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 847088409 434 DLALKQKSELNSRLEEKTNQMAATVKQLEQSEKDLVKQAKTL 475
Cdd:COG4942  191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 281-468 5.57e-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: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  281 QKNyvEELNRQLSATvnnlqAKVDALEKSNTKLTEELAVANNRIITMQE----------------EMERIKEETSYYSEA 344
Cdd:pfam17380 389 QKN--ERVRQELEAA-----RKVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEQERQQQ 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  345 SKKVNKQERTADGQALS---EVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALA--ALRQQLDDL 419
Cdd:pfam17380 462 VERLRQQEEERKRKKLElekEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEE 541

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 847088409  420 RALKHELSFKLQSSDlALKQKSELNSRLE--EKTNQMAATVKQLEQSEKDL 468
Cdd:pfam17380 542 RRKQQEMEERRRIQE-QMRKATEERSRLEamEREREMMRQIVESEKARAEY 591
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
 168-241 2.72e-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: 42.30  E-value: 2.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847088409 168 VKDLPGLRTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNA-LMMEEEGAIISGLLVGLNVIDAnFC 241
Cdd:cd17690  130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVDY-FC 203
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
 289-468 5.14e-04

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 42.84  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  289 NRQLSAT--VNNLQAKVDALEKSNTKLTEELAVAN-------NRI----ITMQEEMERIKEETSYYSE-ASKKVNKQERT 354
Cdd:pfam18971 521 NKGVGATngVSHLEAGFNKVAVFNLPDLNNLAITSfvrrnleNKLtakgLSLQEANKLIKDFLSSNKElAGKALNFNKAV 600

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  355 ADGQ----------ALSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMK----------MLDKDVceKQDALAALRQ 414
Cdd:pfam18971 601 AEAKstgnydevkkAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQansqkdeifaLINKEA--NRDARAIAYT 678

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 847088409  415 QldDLRALKHELSFKLQ--SSDLALKQKS--ELNSRLEEKTNQMAATVKQLEQSEKDL 468
Cdd:pfam18971 679 Q--NLKGIKRELSDKLEkiSKDLKDFSKSfdEFKNGKNKDFSKAEETLKALKGSVKDL 734
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 277-456 6.67e-04

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: 42.06  E-value: 6.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 277 AILDQKNYVEELNRQLSAT---VNNLQAKVDALEKSNTKLTEELAvanNRIITMQ--------------EEMERIKEETS 339
Cdd:COG4942   63 RIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEELA---ELLRALYrlgrqpplalllspEDFLDAVRRLQ 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 340 YYSEASKkvnkqertADGQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDL 419
Cdd:COG4942  140 YLKYLAP--------ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 847088409 420 RAlkhELSFKLQSSDLALKQKSELNSRLEEKTNQMAA 456
Cdd:COG4942  212 AA---ELAELQQEAEELEALIARLEAEAAAAAERTPA 245
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 295-476 9.04e-04

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: 41.28  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  295 TVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIkeETSYYSEASKKvnkqertadGQALSEVKKHLKEETQLR 374
Cdd:pfam09787  41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQEL--EAQQQEEAESS---------REQLQELEEQLATERSAR 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  375 LDIEKELEvqigmRQEMELAmKMLDKDVCEKQDALAALRQQLDDLRALKHELSFKLQSSdlalKQKSELNSRLEEKTNQM 454
Cdd:pfam09787 110 REAEAELE-----RLQEELR-YLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSS----SSQSELENRLHQLTETL 179

                         170       180
                  ....*....|....*....|....*
gi 847088409  455 AATVKQLE--QSEKD-LVKQAKTLN 476
Cdd:pfam09787 180 IQKQTMLEalSTEKNsLVLQLERME 204
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 274-475 2.33e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   274 QITAILDQKNYVEELNRQLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEEtsyYSEASKKVNK--Q 351
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE---LEELSEELREleS 908

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   352 ERTADGQALSEVKKHLkeeTQLRLDIEKeLEVQIGMRQEM-----ELAMKMLDKDVCEKQDALAALRQQLDDLRALKHEL 426
Cdd:TIGR02168  909 KRSELRRELEELREKL---AQLELRLEG-LEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 847088409   427 SfklQSSDLALKQKSELNSRLEEKTNQMA---ATVKQLEQSEKDLVKQAKTL 475
Cdd:TIGR02168  985 G---PVNLAAIEEYEELKERYDFLTAQKEdltEAKETLEEAIEEIDREARER 1033
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 266-477 2.45e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   266 AKCSEGDGQITAILDQKNYVEELNRQLSATVNNLQAKVDALEKSntklteelaVANNRIITMQEEMERIKEETSYYSEAS 345
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSKLEEEVSRIEARL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   346 KKVNK--QERTADGQALSEVKKHLKEETQLRLDIEKELEVQIgmrQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALK 423
Cdd:TIGR02169  815 REIEQklNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI---ENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 847088409   424 HELSFKLqssdlalkqkselnSRLEEKTNQMAATVKQLEQSEKDLVKQAKTLNS 477
Cdd:TIGR02169  892 DELEAQL--------------RELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 327-442 2.77e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 39.23  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 327 MQEEM-----ERIKEETSYYSEASKKVNK----QERTADGQALSEVKKHLKEETQLRLDIEKELEVQI-----GMRQEME 392
Cdd:cd07649   20 MQKEMaefirERIKIEEEYAKNLSKLSQSslaaQEEGTLGEAWAQVKKSLADEAEVHLKFSSKLQSEVekpllNFRENFK 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 847088409 393 LAMKMLDKDVCE--KQDAL--AALRQQLDDLRALKHELSFKLQSSDLALKQKSE 442
Cdd:cd07649  100 KDMKKLDHHIADlrKQLASryAAVEKARKALLERQKDLEGKTQQLEIKLSNKTE 153
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
300-456 3.04e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  300 QAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEETSyyseaskKVNKQERTADGQALSEVKKHLKEETQLRLDIEK 379
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELD-------ELEAQIRGNGGDRLEQLEREIERLERELEERER 359

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 847088409  380 ElevqigmRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALKHELSFKLQSS-DLALKQKSELNSRLEEKTNQMAA 456
Cdd:COG4913   360 R-------RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAlAEAEAALRDLRRELRELEAEIAS 430
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 286-465 3.37e-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: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   286 EELNRQLSATVNNLQAKVDALEKsntKLTEELAvANNRI----ITMQEEMERIKEETSYYSEASKKVNKqERTADGQALS 361
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLDEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSK-ERKLLEERIS 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   362 EVKKHLKEE-------TQLRL-------DIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRAlkhELS 427
Cdd:pfam01576  163 EFTSNLAEEeekakslSKLKNkheamisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA---QLA 239

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 847088409   428 FKLQSSDLALkqkselnSRLEEKTNQMAATVKQLEQSE 465
Cdd:pfam01576  240 KKEEELQAAL-------ARLEEETAQKNNALKKIRELE 270
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 286-475 3.46e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 3.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   286 EELNRQLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEETSYYSEASKKVNKQERtadgQALSEVKK 365
Cdd:TIGR02169  286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD----KLTEEYAE 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409   366 HLKEETQLRLDIEKELEVQIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALKHELSFKLQSSDLALKQKSELNS 445
Cdd:TIGR02169  362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441

                          170       180       190
                   ....*....|....*....|....*....|
gi 847088409   446 RLEEKTNQMAATVKQLEQSEKDLVKQAKTL 475
Cdd:TIGR02169  442 EKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
295-482 4.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 295 TVNNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIKEETSYYSEASKK--VNKQERTadgqalSEVKKHLKEETQ 372
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELT------EEHRKELLEEYT 458

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 373 LRL-DIEKELEVQIGMRQEMELAMKMLDKdVCEKQDALAALRQQLDDLRALKHELS-FKLQSsdlaLKQKSELNSRLEEK 450
Cdd:PRK03918 459 AELkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKkYNLEE----LEKKAEEYEKLKEK 533

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 847088409 451 TNQMAATVKQLE---QSEKDLVKQAKTLNSVAHKL 482
Cdd:PRK03918 534 LIKLKGEIKSLKkelEKLEELKKKLAELEKKLDEL 568
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
278-478 4.71e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 278 ILDQKNYVEELNRQLSATVNNLQAKVDALEKSNTKLtEELavaNNRIITMQEEMERIKEETSYYSEASKKVNKQER---T 354
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EEL---KKKLKELEKRLEELEERHELYEEAKAKKEELERlkkR 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 355 ADGQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEmelamkmLDKDVCEKQDALAALRQQLDDLRALKHELSfklqssd 434
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE-------LKKEIKELKKAIEELKKAKGKCPVCGRELT------- 446

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 847088409 435 laLKQKSELNSRLEEKTNQMAATVKQLEQSEKDLVKQAKTLNSV 478
Cdd:PRK03918 447 --EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
297-486 5.15e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 297 NNLQAKVDALEKSNTKLTEELAVANNRIITMQEEMERIK---------EETSYYSEASKKVNKQERTADGQ------ALS 361
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglvdlsEEAKLLLQQLSELESQLAEARAElaeaeaRLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409 362 EVKKHLKEETQLRLDIEKELEVQIGMRQEMELAMKM--LDKDVCEKQDALAALRQQLDDLRALKHELSFKLQSS-----D 434
Cdd:COG3206  244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELaeLSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASleaelE 323

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 847088409 435 LALKQKSELNSRLEEkTNQMAATVKQLEQSEKDLVKQAKTLNSVAHKLLQKQ 486
Cdd:COG3206  324 ALQAREASLQAQLAQ-LEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
350-474 5.94e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  350 KQERTADGQALSEVKKHLKEETQLRLDIEKELEV--QIGMRQEMELAMKMLDKDVCEKQDALAALRQQLDDLRALKHELs 427
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQL- 694

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 847088409  428 fklqssDLALKQKSELNSRLEEKTNQMAATVKQLEQSEkDLVKQAKT 474
Cdd:COG4913   695 ------EELEAELEELEEELDELKGEIGRLEKELEQAE-EELDELQD 734
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 341-484 9.97e-03

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: 38.78  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847088409  341 YSEASKKVNKQERTAdgQALSEVKKHLKEETQLRLDIEKELEVQIGMRQEmelamkmLDKDVCEKQDALAALRQQLDDLR 420
Cdd:COG3096   521 LAELEQRLRQQQNAE--RLLEEFCQRIGQQLDAAEELEELLAELEAQLEE-------LEEQAAEAVEQRSELRQQLEQLR 591

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847088409  421 ALKHELSFK----LQSSDLALKQKSELNSRLE---EKTNQMAATV---KQLEQSEKDLVKQAKTLNSVAHKLLQ 484
Cdd:COG3096   592 ARIKELAARapawLAAQDALERLREQSGEALAdsqEVTAAMQQLLereREATVERDELAARKQALESQIERLSQ 665
 
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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