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Conserved domains on  [gi|1953291219|ref|XP_038541771|]
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protein RUFY3 isoform X2 [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 1.98e-100

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: 302.69  E-value: 1.98e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219 166 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 241
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
 568-615 6.21e-20

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed 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. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


:

Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 83.24  E-value: 6.21e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953291219 568 ICQLCQEDG---SLTKNVCKNCRGTFCNACSTNELPLPSSI-KPERVCNPCH 615
Cdd:cd15744     1 SCSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-516 1.12e-10

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: 64.96  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 290 RHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEGpKQDRTSEGQALSEARKHLKEETQLRLDVEKE 369
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 370 LEIQISMRQEmelamkmlekdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQ 449
Cdd:COG1196   342 LEEELEEAEE-------------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291219 450 LEQRLRQAERgRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELELKQERERRLQNNRSIPG 516
Cdd:COG1196   409 EEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 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 1.98e-100

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: 302.69  E-value: 1.98e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219 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 1.69e-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: 154.74  E-value: 1.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 121 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 191
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953291219 192 KKLSEYMKALINKKELLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 244
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
 568-615 6.21e-20

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed 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. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 83.24  E-value: 6.21e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953291219 568 ICQLCQEDG---SLTKNVCKNCRGTFCNACSTNELPLPSSI-KPERVCNPCH 615
Cdd:cd15744     1 SCSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
181-243 1.90e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 79.58  E-value: 1.90e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291219  181 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 243
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-516 1.12e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 290 RHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEGpKQDRTSEGQALSEARKHLKEETQLRLDVEKE 369
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 370 LEIQISMRQEmelamkmlekdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQ 449
Cdd:COG1196   342 LEEELEEAEE-------------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291219 450 LEQRLRQAERgRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELELKQERERRLQNNRSIPG 516
Cdd:COG1196   409 EEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
 562-618 8.04e-10

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 55.13  E-value: 8.04e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953291219  562 PSEKPQICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPCHEHL 618
Cdd:smart00064   6 PDEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 311-574 6.53e-09

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: 59.31  E-value: 6.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  311 TKLTEELAVANNRIitlqEEMERVKEGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKD 390
Cdd:TIGR02169  670 RSEPAELQRLRERL----EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  391 VCEKQDALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLE 451
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLT 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  452 QRLRQAERGRQSAELDNRLFK---QDFGDKINSLQLEVEELTRQ--RHQLEL--------ELKQERERRLQNNRSIPGKG 518
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEEleELEAALrdlesrlgDLKKERDELEAQLRELERKI 905

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219  519 SQKPEPKTDGKHKIQEENVKLKKPLDESHRLpsRPVDGQDQPPPSEKPQICQLCQE 574
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKLEALEEELSEI--EDPKGEDEEIPEEELSLEDVQAE 959
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
 569-620 2.10e-07

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 48.15  E-value: 2.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291219 569 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSI---KPERVCNPCHEHLMK 620
Cdd:pfam01363  12 CMICSKPFTFFrrRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTLQK 68
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 292-473 5.84e-06

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: 49.37  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 292 LNATVNNLQAKVDALEK--SNTKLTEELAVannriitlQEEMERVKEGPKQDRTSEGQALSEARKhlKEETQLRLDVEKE 369
Cdd:pfam09731 285 LNSLIAHAHREIDQLSKklAELKKREEKHI--------ERALEKQKEELDKLAEELSARLEEVRA--ADEAQLRLEFERE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 370 L-EIQISMRQEMELAMKMLEKDVCEK-QDALVSLRQQLDdlRALKHELAFKLQssdlgvkqkSELNSRLeEKTNQMAATI 447
Cdd:pfam09731 355 ReEIRESYEEKLRTELERQAEAHEEHlKDVLVEQEIELQ--REFLQDIKEKVE---------EERAGRL-LKLNELLANL 422

                         170       180
                  ....*....|....*....|....*.
gi 1953291219 448 KQLEqrlrQAERGRQSAELDNRLFKQ 473
Cdd:pfam09731 423 KGLE----KATSSHSEVEDENRKAQQ 444
PRK11281 PRK11281
mechanosensitive channel MscK;
285-496 3.87e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.83  E-value: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  285 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVkegpkQDRTSEGQA-----------LSEAR 353
Cdd:PRK11281   123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERA-----QAALYANSQrlqqirnllkgGKVGG 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  354 KHLKEETQLRLDVE-KELEIQISMRQEmELAMKMLEKDVCEKQDALVSLR-----QQLDDLR-----------------A 410
Cdd:PRK11281   187 KALRPSQRVLLQAEqALLNAQNDLQRK-SLEGNTQLQDLLQKQRDYLTARiqrleHQLQLLQeainskrltlsektvqeA 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  411 LKHELAFKLQSSDLgVKQKSELNSRLE-------EKTNQMAA---TIKQLEQRLRQAERG--------RQSAELDNRLFK 472
Cdd:PRK11281   266 QSQDEAARIQANPL-VAQELEINLQLSqrllkatEKLNTLTQqnlRVKNWLDRLTQSERNikeqisvlKGSLLLSRILYQ 344

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1953291219  473 Q-----------DFGDKINSLQLEVEELTRQRHQL 496
Cdd:PRK11281   345 QqqalpsadlieGLADRIADLRLEQFEINQQRDAL 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 1.98e-100

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: 302.69  E-value: 1.98e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219 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 9.85e-97

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: 293.04  E-value: 9.85e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219 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 1.66e-93

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: 1.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17681     1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953291219 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 2.30e-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: 279.10  E-value: 2.30e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  86 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 165
Cdd:cd17694     1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219 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 1.69e-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: 154.74  E-value: 1.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 121 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 191
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953291219 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 7.83e-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: 131.75  E-value: 7.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  89 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLG--QNKSFWGPLELVEKLVPEAAeiTA 166
Cdd:cd17684     1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IA 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291219 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 3.87e-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: 121.38  E-value: 3.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  97 SIKGLIESALNLGR-------TLDSDYAPLQQFFVVMEHCLKHGLKAKKtFLGQNKSFWGPLELVEKLVPEAAEITA--S 167
Cdd:cd17671     2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKQAirD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291219 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 1.85e-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: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  89 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQN--KSFWGPLELVEKLVPEAAeiTA 166
Cdd:cd17700     1 NLITVCRFSVKTLIDRSCF--ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHNC--IC 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953291219 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 7.31e-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: 7.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  89 NLMNMAKLSIKGLIESALnlGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQnKSFWGPLELVEKLVPEaaEIT 165
Cdd:cd17699     1 NLITVCRFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVPN--NCI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219 166 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 241
Cdd:cd17699    76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
 568-615 6.21e-20

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed 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. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 83.24  E-value: 6.21e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953291219 568 ICQLCQEDG---SLTKNVCKNCRGTFCNACSTNELPLPSSI-KPERVCNPCH 615
Cdd:cd15744     1 SCSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
181-243 1.90e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 79.58  E-value: 1.90e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291219  181 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 243
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
 569-615 2.34e-16

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed 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 homologue 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 termed 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. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277261 [Multi-domain]  Cd Length: 58  Bit Score: 73.57  E-value: 2.34e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1953291219 569 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPCH 615
Cdd:cd15721    10 CQQCEKEFSLSrrKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
 98-237 5.11e-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: 75.34  E-value: 5.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  98 IKGLIESALNLGRTLDSDYAP-LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLE-LVEKLVPEA---AEITASVKDLP 172
Cdd:cd17682     2 LKGCVLDLKSEFGEITDPDNPyLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219 173 GLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEE-GAIIAGLLVGLNVID 237
Cdd:cd17682    82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEIlSEILLSLLYQLNEIN 147
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 569-625 6.42e-14

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed 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.


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 66.97  E-value: 6.42e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953291219 569 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPCHEHLMKQYSSS 625
Cdd:cd15759    13 CKLCEKEFSLSkrKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 87-233 1.33e-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: 69.16  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  87 RMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAK-----KTFLGQN------KSFWGPLELV- 154
Cdd:cd17679     1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKfiskvSSVFSGDvdklpePNFWPLLLKFs 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 155 EKlvpeaaEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGL 233
Cdd:cd17679    81 HR------DVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGL 154
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 569-623 1.97e-13

FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed 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 homologue 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.


Pssm-ID: 277297 [Multi-domain]  Cd Length: 71  Bit Score: 65.47  E-value: 1.97e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291219 569 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPCHEHLMKQYS 623
Cdd:cd15758    15 CKQCEKEFSISrrKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
 171-236 2.32e-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: 65.33  E-value: 2.32e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291219 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 3.56e-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: 3.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 126 MEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKK 205
Cdd:cd17697    35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1953291219 206 ELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVI 236
Cdd:cd17697   115 ELTGEWYYARSpFLSPELRSDILDSLYELNGV 146
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-516 1.12e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 290 RHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEGpKQDRTSEGQALSEARKHLKEETQLRLDVEKE 369
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 370 LEIQISMRQEmelamkmlekdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQ 449
Cdd:COG1196   342 LEEELEEAEE-------------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291219 450 LEQRLRQAERgRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELELKQERERRLQNNRSIPG 516
Cdd:COG1196   409 EEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-509 1.94e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 290 RHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERvkegpkqdrtsEGQALSEARKHLKEETQLRLDVEKE 369
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-----------LELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 370 LEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQ 449
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 450 LEQRLRQAErgRQSAELDNRLfkQDFGDKINSLQLEVEELTRQRHQLELELKQERERRLQ 509
Cdd:COG1196   384 LAEELLEAL--RAAAELAAQL--EELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 97-218 2.78e-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: 58.79  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  97 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKktflgqNKSFWGpleLVEKLVPEAAEItaSVKDLPGLKT 176
Cdd:cd17680    12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRG------NRGYWP---FVKEFTHKETIK--QIENLPNVTT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953291219 177 PVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALM 218
Cdd:cd17680    81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
 127-237 2.84e-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: 59.22  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 127 EHCLKHGLKAKK-TFLGQNKSFwGPLELVEKLVPEAAEITASVKDL------PGLKTPVGRGRA-------------WLR 186
Cdd:cd17687    31 DACLLHGLRKRAlGLFRSSSTF-SLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIR 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953291219 187 LALMQKKLSEYMKALINKKellSEFYEPNALMME-EEGAIIAGLLVGLNVID 237
Cdd:cd17687   110 IALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
 569-615 6.75e-10

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 54.85  E-value: 6.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953291219 569 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPS--SIKPERVCNPCH 615
Cdd:cd00065     2 CMLCGKKFSLFrrRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
 562-618 8.04e-10

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 55.13  E-value: 8.04e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953291219  562 PSEKPQICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPCHEHL 618
Cdd:smart00064   6 PDEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 92-240 2.04e-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: 56.63  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  92 NMAKLSIKGLIESALNLGRTLDSDYAP-------LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEI 164
Cdd:cd17698     2 SQLQKIIRDLQDCVTELKKEFEETGEPitddsttLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLNDG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291219 165 TASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEP-NALMMEEEGAIIAGLLVGLNviDANF 240
Cdd:cd17698    82 IRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPrSVFLNHKYSSDIINSLYDLN--EVQF 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 292-514 2.24e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 292 LNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEgpkqDRTSEGQALSEARKHLKEETQLRLDVEKELE 371
Cdd:COG1196   279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE----ELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 372 IQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLE 451
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953291219 452 QRLRQAERGRQSAELdnrlfkqdfgdKINSLQLEVEELTRQRHQLELELKQERERRLQNNRSI 514
Cdd:COG1196   435 EEEEEEEEALEEAAE-----------EEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
 132-241 4.69e-09

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: 56.25  E-value: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 132 HGLKAKktflgQNKS-FWGPL----ELVEKLVPEAAEITA---SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALIN 203
Cdd:cd17677    65 HGLQTK-----QGKSaLWSHLlayqENEERLKPLPESLLFdmkNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1953291219 204 KKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 241
Cdd:cd17677   140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVDY-FC 177
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
 119-239 5.73e-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: 5.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 119 LQQFFVVMEHCLKHGLKAKKTFLGQNkSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVG-RGRAWLRLALMQKKLSEY 197
Cdd:cd17686    21 LQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGRLWLRQSLQQHCLSSQ 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953291219 198 MKALINKKELLSEFYEPNALMMEEEGAiiAGLLVGLNVIDAN 239
Cdd:cd17686   100 LQWLVSDKELLRKYYEDEAFLRQEGYA--TALLICLTAVELN 139
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 311-574 6.53e-09

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: 59.31  E-value: 6.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  311 TKLTEELAVANNRIitlqEEMERVKEGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKD 390
Cdd:TIGR02169  670 RSEPAELQRLRERL----EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  391 VCEKQDALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLE 451
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLT 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  452 QRLRQAERGRQSAELDNRLFK---QDFGDKINSLQLEVEELTRQ--RHQLEL--------ELKQERERRLQNNRSIPGKG 518
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEEleELEAALrdlesrlgDLKKERDELEAQLRELERKI 905

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219  519 SQKPEPKTDGKHKIQEENVKLKKPLDESHRLpsRPVDGQDQPPPSEKPQICQLCQE 574
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKLEALEEELSEI--EDPKGEDEEIPEEELSLEDVQAE 959
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
 568-615 1.18e-08

FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.


Pssm-ID: 277274 [Multi-domain]  Cd Length: 59  Bit Score: 51.76  E-value: 1.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953291219 568 ICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLP--SSIKPERVCNPCH 615
Cdd:cd15735     8 VCMRCRTAFTFTnrKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
 569-614 2.31e-08

FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.


Pssm-ID: 277269 [Multi-domain]  Cd Length: 63  Bit Score: 50.86  E-value: 2.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1953291219 569 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPC 614
Cdd:cd15730    12 CMACGKGFSVTvrKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDAC 59
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 261-512 2.51e-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: 2.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  261 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEG 337
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  338 PKQDRTSEGQALSEAR---KHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQD-------ALVSLRQQLDD 407
Cdd:TIGR02168  735 LARLEAEVEQLEERIAqlsKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkalreALDELRAELTL 814

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  408 LRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEVE 487
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEALA 890

                          250       260
                   ....*....|....*....|....*
gi 1953291219  488 ELTRQRHQLELELKQERERRLQNNR 512
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRR 915
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-508 4.65e-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: 4.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 276 TAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEgpkqDRTSEGQALSEA 352
Cdd:COG1196   267 AELEELRLELEELELELEeaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE----ELEELEEELEEL 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 353 RKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAfkLQSSDLGVKQKSEL 432
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE--EAEEALLERLERLE 420

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219 433 NSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDfgDKINSLQLEVEELTRQRHQLELELKQERERRL 508
Cdd:COG1196   421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL--ELLAELLEEAALLEAALAELLEELAEAAARLL 494
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
 168-241 6.80e-08

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: 53.52  E-value: 6.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953291219 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 ...
 269-507 1.11e-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: 55.06  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  269 SEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEGPKQ---DRTSE 345
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESlerRIAAT 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  346 GQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLG 425
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  426 VKQKSELNSRLEEKTNQMAATIKQLEQRLRqaERGRQSAELDNRLfKQDFGDKINSLQLEVEELTRQRHQL-------EL 498
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-ENKIEDDEEEARRRLKRLENKIKELgpvnlaaIE 993


                   ....*....
gi 1953291219  499 ELKQERERR 507
Cdd:TIGR02168  994 EYEELKERY 1002
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
300-506 1.25e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  300 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVkegpkqdrtsegQALSEARKHLKEETQLRLDVEkELEIQIsmrQE 379
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL------------QERREALQRLAEYSWDEIDVA-SAEREI---AE 672

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  380 MELAMKMLEKDvcekQDALVSLRQQLDDLRALKHELAFKLqssdlgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQAER 459
Cdd:COG4913    673 LEAELERLDAS----SDDLAALEEQLEELEAELEELEEEL-------DELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953291219  460 GR---QSAELDNRLFKQDFGDKINSLQlevEELTRQRHQLELELKQERER 506
Cdd:COG4913    742 LArleLRALLEERFAAALGDAVERELR---ENLEERIDALRARLNRAEEE 788
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
 569-614 1.37e-07

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.


Pssm-ID: 277273 [Multi-domain]  Cd Length: 61  Bit Score: 48.48  E-value: 1.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953291219 569 CQLCQEDGS--LTKNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPC 614
Cdd:cd15734    11 CSVCKRPFSprLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
 569-620 2.10e-07

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 48.15  E-value: 2.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291219 569 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSI---KPERVCNPCHEHLMK 620
Cdd:pfam01363  12 CMICSKPFTFFrrRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTLQK 68
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
 569-614 2.22e-07

FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 47.97  E-value: 2.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953291219 569 CQLCQED--GSLTKNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPC 614
Cdd:cd15732    11 CYGCEREfwLASRKHHCRNCGNVFCGSCCNQKLPVPSQqlFEPSRVCKSC 60
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
 559-614 3.26e-07

FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 47.72  E-value: 3.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953291219 559 QPP---PSEKPQICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSI--KPERVCNPC 614
Cdd:cd15731     1 DPPlwvPDEACPQCMACSAPFTVLrrRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 273-506 4.79e-07

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: 52.46  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 273 GQITAILDQKNYVEELNRHLNAT---VNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEGPKQDRTSEgQAL 349
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELekeLAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-AEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 350 SEARKHLKEETQLRLDVEKELEIQISMR--------QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS 421
Cdd:COG4942    96 RAELEAQKEELAELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 422 SDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERgrqsaeldnrlfkqdfgdKINSLQLEVEELTRQRHQLELELK 501
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAA------------------ELAELQQEAEELEALIARLEAEAA 237


                  ....*
gi 1953291219 502 QERER 506
Cdd:COG4942   238 AAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-520 5.21e-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: 53.14  E-value: 5.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  272 DGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEgpKQDRTSEgqALSE 351
Cdd:TIGR02168  266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES--KLDELAE--ELAE 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  352 ARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAlkhelafklqssdlgvkQKSE 431
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-----------------EIER 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  432 LNSRLEektnQMAATIKQLEQRLRQAERGRQSAELdnrlfkQDFGDKINSLQLEVEELTRQRHQLELELKQERERRLQNN 511
Cdd:TIGR02168  405 LEARLE----RLEDRRERLQQEIEELLKKLEEAEL------KELQAELEELEEELEELQEELERLEEALEELREELEEAE 474


                   ....*....
gi 1953291219  512 RSIPGKGSQ 520
Cdd:TIGR02168  475 QALDAAERE 483
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 329-509 6.25e-07

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: 52.65  E-value: 6.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  329 EEMERVKEGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDV--CEKQDALVSLRQQLD 406
Cdd:COG3096    423 EKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWQTARELLR 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  407 DLRALKHelafklqssdlgvkqkselnsrLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINsLQLEV 486
Cdd:COG3096    503 RYRSQQA----------------------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELL 559

                          170       180
                   ....*....|....*....|...
gi 1953291219  487 EELTRQRHQLELELKQERERRLQ 509
Cdd:COG3096    560 AELEAQLEELEEQAAEAVEQRSE 582
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-465 9.55e-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: 9.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 274 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKE---GPKQDRTSEGQALS 350
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelaEAEEALLEAEAELA 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 351 EARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKS 430
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1953291219 431 ELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAE 465
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
RUN_SGSM1 cd17703
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ...
 98-232 1.66e-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: 48.85  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  98 IKGLIESALNLgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKT-FLGQNK----------SFWGPLELVEKL--------- 157
Cdd:cd17703     3 VKQIMEEAVTR-KFVHEDSSHIISFCAAVEACVLHGLKRRAAgFLRSNKiaalfmkvgkSFPPAEELCRKVqeleqllen 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 158 ----VPEAAEITASVKDLPGLkTPVGRGRAWLRLALMQKKLSEYMKALInkkELLSEFYEPNALMMEE-EGAIIAGLLVG 232
Cdd:cd17703    82 krnqMQGLQENVRKMPKLPNL-SPQAIKHLWIRTALFEKVLDKIVHYLV---ENSSKYYEKEALLMDPvDGPILASLLVG 157
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
 569-618 2.31e-06

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.


Pssm-ID: 277260 [Multi-domain]  Cd Length: 61  Bit Score: 45.07  E-value: 2.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953291219 569 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPS-SI-KPERVCNPCHEHL 618
Cdd:cd15720     8 CHRCRVQFGVFqrKHHCRACGQVFCGKCSSKSSTIPKfGIeKEVRVCDPCYEKL 61
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
 569-618 2.36e-06

FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.


Pssm-ID: 277259 [Multi-domain]  Cd Length: 65  Bit Score: 45.07  E-value: 2.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953291219 569 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPS--SIKPERVCNPCHEHL 618
Cdd:cd15719    12 CTGCSVRFSLTerRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 269-516 3.21e-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: 50.45  E-value: 3.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  269 SEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTE---------------ELAVANNRIITLQEEMER 333
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvkekigeleaEIASLERSIAEKERELED 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  334 VKEGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQLDDLR- 409
Cdd:TIGR02169  320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREKLEKLKr 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  410 ---ALKHELAFKLQSSDLGVKQKSELNS---RLEEKTNQMAATIKQLEQRLRQAERGRQSAELDnrlfKQDFGDKINSLQ 483
Cdd:TIGR02169  400 einELKRELDRLQEELQRLSEELADLNAaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLK 475

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1953291219  484 LEVEELTRQRHQLELELKQERERRLQNNRSIPG 516
Cdd:TIGR02169  476 EEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
 559-614 4.34e-06

FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.


Pssm-ID: 277266 [Multi-domain]  Cd Length: 64  Bit Score: 44.29  E-value: 4.34e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953291219 559 QPP--PSEKPQICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLP--SSIKPERVCNPC 614
Cdd:cd15727     1 EPPwvPDKECPVCMSCKKKFDFFkrRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
 561-615 4.65e-06

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277257 [Multi-domain]  Cd Length: 61  Bit Score: 44.28  E-value: 4.65e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953291219 561 PPSEKPqICQLCQEdgslTK-NV------CKNCRGTFCNACSTNELPLPS-SIKPERVCNPCH 615
Cdd:cd15717     4 PDSEAP-VCMHCKK----TKfTAinrrhhCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 292-473 5.84e-06

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: 49.37  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 292 LNATVNNLQAKVDALEK--SNTKLTEELAVannriitlQEEMERVKEGPKQDRTSEGQALSEARKhlKEETQLRLDVEKE 369
Cdd:pfam09731 285 LNSLIAHAHREIDQLSKklAELKKREEKHI--------ERALEKQKEELDKLAEELSARLEEVRA--ADEAQLRLEFERE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 370 L-EIQISMRQEMELAMKMLEKDVCEK-QDALVSLRQQLDdlRALKHELAFKLQssdlgvkqkSELNSRLeEKTNQMAATI 447
Cdd:pfam09731 355 ReEIRESYEEKLRTELERQAEAHEEHlKDVLVEQEIELQ--REFLQDIKEKVE---------EERAGRL-LKLNELLANL 422

                         170       180
                  ....*....|....*....|....*.
gi 1953291219 448 KQLEqrlrQAERGRQSAELDNRLFKQ 473
Cdd:pfam09731 423 KGLE----KATSSHSEVEDENRKAQQ 444
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
 580-615 1.82e-05

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 42.42  E-value: 1.82e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1953291219 580 KNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPCH 615
Cdd:cd15733    23 KHHCRNCGNVFCADCSNYKLPIPDEqlYDPVRVCNSCY 60
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
296-514 2.29e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 296 VNNLQAKVDALEKSNTKLTE----ELAVANNRIITLQEEMERVKEGpKQDRTSEGQALSEARKHLKEETQLRLDVEKELE 371
Cdd:COG4717    48 LERLEKEADELFKPQGRKPElnlkELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 372 IQISMRQEMELAMKMLEKdvcekQDALVSLRQQLDDLRALKHELAFKLQSSDlgvKQKSELNSRLEEKTNQMAATIKQLE 451
Cdd:COG4717   127 LLPLYQELEALEAELAEL-----PERLEELEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATEEELQDLA 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291219 452 QRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEELTRQRHQLELEL-KQERERRLQNNRSI 514
Cdd:COG4717   199 EELEELQQRLAELE-----------EELEEAQEELEELEEELEQLENELeAAALEERLKEARLL 251
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 292-505 2.70e-05

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: 47.48  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  292 LNATVNNLQAKVDALEKSNTKLTEELAVANNRI----ITLQEEMERVKEGPKQdRTSEGQALSEARKHLKEETQLRldve 367
Cdd:pfam01576  129 TEAKIKKLEEDILLLEDQNSKLSKERKLLEERIseftSNLAEEEEKAKSLSKL-KNKHEAMISDLEERLKKEEKGR---- 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  368 keleiqismrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATI 447
Cdd:pfam01576  204 ----------QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953291219  448 KQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVEE-LTRQRHQLELELKQERE 505
Cdd:pfam01576  274 SELQEDLESERAARNKAEKQRR----DLGEELEALKTELEDtLDTTAAQQELRSKREQE 328
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 295-499 2.85e-05

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: 46.29  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 295 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEiqi 374
Cdd:pfam09787  41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELE--- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 375 SMRQEMElamKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSdlgvKQKSELNSRLEEKTNQMAATIKQLEQrl 454
Cdd:pfam09787 118 RLQEELR---YLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSS----SSQSELENRLHQLTETLIQKQTMLEA-- 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1953291219 455 RQAERgrqsaeldnrlfkqdfgdkiNSLQLEVEELTRQRHQLELE 499
Cdd:pfam09787 189 LSTEK--------------------NSLVLQLERMEQQIKELQGE 213
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
 569-615 3.50e-05

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.


Pssm-ID: 277299 [Multi-domain]  Cd Length: 59  Bit Score: 41.90  E-value: 3.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953291219 569 CQLCQEDGSLTK--NVCKNCRGTFCNACSTNELPLPSSI---KPERVCNPCH 615
Cdd:cd15760     8 CDVCRKKFGLFKrrHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 342-514 3.52e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 342 RTSEGQALSEARKHLKEETQLRLDVEKELEIQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS 421
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAEL---EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 422 SDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDnrlfKQDFGDKINSLQLEVEELTRQRHQLELELK 501
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         170
                  ....*....|...
gi 1953291219 502 QERERRLQNNRSI 514
Cdd:COG1196   376 EAEEELEELAEEL 388
PRK11281 PRK11281
mechanosensitive channel MscK;
285-496 3.87e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.83  E-value: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  285 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVkegpkQDRTSEGQA-----------LSEAR 353
Cdd:PRK11281   123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERA-----QAALYANSQrlqqirnllkgGKVGG 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  354 KHLKEETQLRLDVE-KELEIQISMRQEmELAMKMLEKDVCEKQDALVSLR-----QQLDDLR-----------------A 410
Cdd:PRK11281   187 KALRPSQRVLLQAEqALLNAQNDLQRK-SLEGNTQLQDLLQKQRDYLTARiqrleHQLQLLQeainskrltlsektvqeA 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  411 LKHELAFKLQSSDLgVKQKSELNSRLE-------EKTNQMAA---TIKQLEQRLRQAERG--------RQSAELDNRLFK 472
Cdd:PRK11281   266 QSQDEAARIQANPL-VAQELEINLQLSqrllkatEKLNTLTQqnlRVKNWLDRLTQSERNikeqisvlKGSLLLSRILYQ 344

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1953291219  473 Q-----------DFGDKINSLQLEVEELTRQRHQL 496
Cdd:PRK11281   345 QqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
 569-615 6.64e-05

FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 40.57  E-value: 6.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953291219 569 CQLCQEDGSLTKNV--CKNCRGTFCNACSTNELPLPS-SIKPERVCNPCH 615
Cdd:cd15749     2 CFGCAAKFSLFKKEcgCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
 168-241 7.17e-05

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: 44.23  E-value: 7.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953291219 168 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 241
Cdd:cd17690   130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVDY-FC 203
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 245-502 9.94e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 9.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  245 EDLDSQVGVIDFSMylkDGNSSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRI 324
Cdd:TIGR02168  298 SRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  325 ITLQEEMERVKEgpKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQismrQEMELAMKMLEKDVCEkqdalvsLRQQ 404
Cdd:TIGR02168  375 EELEEQLETLRS--KVAQLELQIASLNNEIERLEARLERLEDRRERLQQ----EIEELLKKLEEAELKE-------LQAE 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  405 LDDLRALKHELafklqssdlgVKQKSELNSRLEEKTNQmaatIKQLEQRLRQAErgRQSAELDNRLfkqdfgDKINSLQL 484
Cdd:TIGR02168  442 LEELEEELEEL----------QEELERLEEALEELREE----LEEAEQALDAAE--RELAQLQARL------DSLERLQE 499

                          250
                   ....*....|....*...
gi 1953291219  485 EVEELTRQRHQLELELKQ 502
Cdd:TIGR02168  500 NLEGFSEGVKALLKNQSG 517
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
 568-614 1.53e-04

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; 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. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 39.79  E-value: 1.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953291219 568 ICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKP--ERVCNPC 614
Cdd:cd15745     1 ACAICAKAFSLFrrKYVCRLCGGVVCHSCSSEDLVLSVPDTCiyLRVCKTC 51
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 304-458 2.21e-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: 44.34  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 304 DALEKSNTKLTEELAVANNRI----ITLQEEMERVKEGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQE 379
Cdd:pfam17380 431 EARQREVRRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE 510

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 380 MELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQKSELNSRLE--EKTNQMAATIKQLEQRLR 455
Cdd:pfam17380 511 EERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKATEERSRLEamEREREMMRQIVESEKARA 589


                  ...
gi 1953291219 456 QAE 458
Cdd:pfam17380 590 EYE 592
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 317-513 4.04e-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: 43.21  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 317 LAVANNRIITLQEEMERVKEGPKQDRtsegQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQD 396
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 397 ALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQL-EQRLRQAERGRQSAELDNRLfKQDF 475
Cdd:COG4942    91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAELAAL-RAEL 169

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1953291219 476 GDKINSLQLEVEELTRQRHQLElELKQERERRLQNNRS 513
Cdd:COG4942   170 EAERAELEALLAELEEERAALE-ALKAERQKLLARLEK 206
mukB PRK04863
chromosome partition protein MukB;
349-515 4.65e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  349 LSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 426
Cdd:PRK04863   444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  427 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAErGRQSAELDNRLFKQDF----GDKINSLQLEVEELTRQRHQLELELK 501
Cdd:PRK04863   519 RMRlSELEQRLRQQ--------QRAERLLAEFC-KRLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589

                          170
                   ....*....|....
gi 1953291219  502 QERERRLQNNRSIP 515
Cdd:PRK04863   590 QLQARIQRLAARAP 603
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 260-508 4.99e-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: 43.19  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 260 LKDGNSSKGSEGDGQITAILDQKNYVEELNRHLNATvnNLQAKVDALEKSNTkltEELAVANNRIitlqEEMERVKEGPK 339
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQ---EEIAMEISRM----RELERLQMERQ 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 340 QDRTSEGQALSEARKH--LKEETQLRLDVEKELEIQISMRQE--MELAMKMLEKDVC-----------EKQDALVSLRQQ 404
Cdd:pfam17380 389 QKNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEeaRQREVRRLEEERAremervrleeqERQQQVERLRQQ 468

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 405 LDDLRALKHELAFKLQSSDLGVKQK-----SELNSR----LEEKtNQMAATIKQLEQRLRQ--AERGRQSAELDNRlfKQ 473
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRrkileKELEERkqamIEEE-RKRKLLEKEMEERQKAiyEEERRREAEEERR--KQ 545

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1953291219 474 DFGDKINSLQLEVEELTRQRHQLElelKQERERRL 508
Cdd:pfam17380 546 QEMEERRRIQEQMRKATEERSRLE---AMEREREM 577
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 311-509 6.49e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 6.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  311 TKLTEELAVANNRIITLQEEMERV----KEGPKQDRTSEGQA-LSEARKHLKEE-TQLRLDVE-KELEIQISMRQEMELA 383
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLedilNELERQLKSLERQAeKAERYKELKAElRELELALLvLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  384 MKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS--SDLG--VKQKSELNSRLEEKTNQMAATIKQLEQRLRQAER 459
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqKELYalANEISRLEQQKQILRERLANLERQLEELEAQLEE 327

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953291219  460 GRQSAELDNRLFKQdFGDKINSLQLEVEELtRQRHQLELELKQERERRLQ 509
Cdd:TIGR02168  328 LESKLDELAEELAE-LEEKLEELKEELESL-EAELEELEAELEELESRLE 375
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 286-508 7.16e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 7.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  286 EELNRHLNATVNNLQA----KVDALEKSNTK--------LTEELAVANNRIITLQEEMERVKEGPKQDRTSE------GQ 347
Cdd:pfam15921  141 EDLRNQLQNTVHELEAakclKEDMLEDSNTQieqlrkmmLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfrslGS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  348 ALSEARKHLKEETQLR----LDVEKELEIQISMRQ-EMELAMKM----LEKDVCEKQDALVSLRQQLDDLRALKHELAFK 418
Cdd:pfam15921  221 AISKILRELDTEISYLkgriFPVEDQLEALKSESQnKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQ 300

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  419 L----------------QSSDLGvKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSL 482
Cdd:pfam15921  301 LeiiqeqarnqnsmymrQLSDLE-STVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379

                          250       260
                   ....*....|....*....|....*.
gi 1953291219  483 QLEVEELtrQRHQLELELKQERERRL 508
Cdd:pfam15921  380 QKLLADL--HKREKELSLEKEQNKRL 403
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 347-536 7.48e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.90  E-value: 7.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  347 QALSEARKHLKEETQLRLDVEKELEiqismrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAL---KHELAFKLQssd 423
Cdd:pfam12128  600 EELRERLDKAEEALQSAREKQAAAE------EQLVQANGELEKASREETFARTALKNARLDLRRLfdeKQSEKDKKN--- 670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  424 lgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDF-----GDKINSLQLEVEELTRQRHQLEL 498
Cdd:pfam12128  671 ---KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqvveGALDAQLALLKAAIAARRSGAKA 747

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1953291219  499 ELKQERErrlQNNRSIPGKGsqkPEPKTDGKHKIQEEN 536
Cdd:pfam12128  748 ELKALET---WYKRDLASLG---VDPDVIAKLKREIRT 779
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
286-465 9.41e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 286 EELNRhLNATVNNLQAKVDALEKSN--TKLTEELAVANNRIITLQEEMERVKEgpkqDRTSEGQALSEARKHLKEETQLR 363
Cdd:COG3206   182 EQLPE-LRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARA----ELAEAEARLAALRAQLGSGPDAL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 364 LDVEKELEIQISMRQEMELAMKM--LEKDVCEKQDALVSLRQQLDDLRA-LKHELAFKLQSSDLGVK----QKSELNSRL 436
Cdd:COG3206   257 PELLQSPVIQQLRAQLAELEAELaeLSARYTPNHPDVIALRAQIAALRAqLQQEAQRILASLEAELEalqaREASLQAQL 336

                         170       180
                  ....*....|....*....|....*....
gi 1953291219 437 EEkTNQMAATIKQLEQRLRQAERGRQSAE 465
Cdd:COG3206   337 AQ-LEARLAELPELEAELRRLEREVEVAR 364
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 287-512 9.57e-04

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: 42.40  E-value: 9.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 287 ELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEGPKQDRTSEGQALSEARKHL---------- 356
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTcsleellrte 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 357 -----KEETQLRL---DVEK---ELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQ---QLDDLRALKHELAFKLQSS 422
Cdd:pfam05483 369 qqrleKNEDQLKIitmELQKkssELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekIAEELKGKEQELIFLLQAR 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 423 DlgvKQKSELNSRLEEKTNQMAATIKQLEQrlrqaergrQSAELDNRLFKQ-DFGDKINSLQLEVEELTRQRHQLELELK 501
Cdd:pfam05483 449 E---KEIHDLEIQLTAIKTSEEHYLKEVED---------LKTELEKEKLKNiELTAHCDKLLLENKELTQEASDMTLELK 516

                         250
                  ....*....|.
gi 1953291219 502 QERERRLQNNR 512
Cdd:pfam05483 517 KHQEDIINCKK 527
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 347-503 1.00e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 347 QALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD------DLRALKHELAF-KL 419
Cdd:COG1579    24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQKEIESlKR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 420 QSSDLGvKQKSELNSRLEEKTNQMAATIKQLEQrlRQAERGRQSAELDnrlfkqdfgDKINSLQLEVEELTRQRHQLELE 499
Cdd:COG1579   104 RISDLE-DEILELMERIEELEEELAELEAELAE--LEAELEEKKAELD---------EELAELEAELEELEAEREELAAK 171


                  ....
gi 1953291219 500 LKQE 503
Cdd:COG1579   172 IPPE 175
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 274-487 1.04e-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: 42.40  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 274 QITAILDQKNY----VEELNRHL-NATVNN--LQAKVDALEKSNTKLTEElavANNRIITLQEEMERVKEGPKQdrtsEG 346
Cdd:pfam05483 458 QLTAIKTSEEHylkeVEDLKTELeKEKLKNieLTAHCDKLLLENKELTQE---ASDMTLELKKHQEDIINCKKQ----EE 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 347 QALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGV 426
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953291219 427 KQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAeldnrlfKQDFGDKINSLQLEVE 487
Cdd:pfam05483 611 EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA-------KQKFEEIIDNYQKEIE 664
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
 580-620 1.27e-03

FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.


Pssm-ID: 277278 [Multi-domain]  Cd Length: 73  Bit Score: 37.71  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1953291219 580 KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPCHEHLMK 620
Cdd:cd15739    26 KHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 292-502 1.44e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 292 LNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEgpkqdrtsEGQALSEARKHLKEETQLRLDVEKELE 371
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ--------EIKNLESQINDLESKIQNQEKLNQQKD 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 372 IQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLE 451
Cdd:TIGR04523 412 EQI---KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953291219 452 QRLRQAER-----GRQSAELDNRLfkQDFGDKINSLQLEVEELTRQRHQLELELKQ 502
Cdd:TIGR04523 489 KELKSKEKelkklNEEKKELEEKV--KDLTKKISSLKEKIEKLESEKKEKESKISD 542
PLN02939 PLN02939
transferase, transferring glycosyl groups
 300-507 1.53e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.81  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 300 QAKVDALEKSNTKLTEELAVaNNRIITLqeEMERVKEGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQE 379
Cdd:PLN02939  149 QARLQALEDLEKILTEKEAL-QGKINIL--EMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLS 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 380 MELAMKMLEKdvcekqdalVSLRqqlDDLRALKHELafklqssdLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAer 459
Cdd:PLN02939  226 KELDVLKEEN---------MLLK---DDIQFLKAEL--------IEVAETEERVFKLEKERSLLDASLRELESKFIVA-- 283

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953291219 460 grQSAELDNRLFKQD-FGDKINSLQLEVEELTRQRHQLELELKQERERR 507
Cdd:PLN02939  284 --QEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLR 330
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 378-506 1.57e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 378 QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDlgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQA 457
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKLQAEIAEAEAEIEERREELGERARAL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953291219 458 ERGRQSAELDNRLFK-QDFGDKINSLQLeVEELTRQRHQLELELKQERER 506
Cdd:COG3883    96 YRSGGSVSYLDVLLGsESFSDFLDRLSA-LSKIADADADLLEELKADKAE 144
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
271-541 2.10e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 271 GDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEgpkqdrtsegqALS 350
Cdd:COG4372     1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE-----------ELE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 351 EARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKS 430
Cdd:COG4372    70 QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 431 ELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRL-----FKQDFGDKINSLQLEVEELTRQRHQLELELKQERE 505
Cdd:COG4372   150 EELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLkeanrNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1953291219 506 RRLQNNRSIPGKGSQKPEPKTDGKHKIQEENVKLKK 541
Cdd:COG4372   230 KLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 328-549 2.25e-03

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: 41.26  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 328 QEEMERVKEGPKQDRTSEGQALSEARKHLK-----EETQLRLDVEKELE-IQIS--------MRQEmELAMKM-----LE 388
Cdd:pfam17380 303 QEKEEKAREVERRRKLEEAEKARQAEMDRQaaiyaEQERMAMERERELErIRQEerkrelerIRQE-EIAMEIsrmreLE 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 389 KDVCEKQDALVSLRQQLDDLRALK-----HELAFKLQSSDLGVKQKSELNSR------LEEKTNQMAATIKQLEQ-RLRQ 456
Cdd:pfam17380 382 RLQMERQQKNERVRQELEAARKVKileeeRQRKIQQQKVEMEQIRAEQEEARqrevrrLEEERAREMERVRLEEQeRQQQ 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 457 AERGRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRHQLELELKQERERRLQNNRSIPGKGSQKPEPKT--DGKHKIQE 534
Cdd:pfam17380 462 VERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAE 539

                         250
                  ....*....|....*
gi 1953291219 535 ENVKLKKPLDESHRL 549
Cdd:pfam17380 540 EERRKQQEMEERRRI 554
mukB PRK04863
chromosome partition protein MukB;
286-509 2.42e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  286 EELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKegpKQDRTSEGQALSEARKHLKEETQLRLD 365
Cdd:PRK04863   836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLN---LLADETLADRVEEIREQLDEAEEAKRF 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  366 VEK------ELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ---LDDLRALKHELAFKLQSSDLGvkQKSELNSRL 436
Cdd:PRK04863   913 VQQhgnalaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVQRRAHFSYEDAAEMLA--KNSDLNEKL 990

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  437 EEKTNQMAATIKQLEQRLRQAE-------------RGRQSAELDNRL-FKQDFGDKINSLQLEVEELTR-QRHQLELELK 501
Cdd:PRK04863   991 RQRLEQAEQERTRAREQLRQAQaqlaqynqvlaslKSSYDAKRQMLQeLKQELQDLGVPADSGAEERARaRRDELHARLS 1070


                   ....*...
gi 1953291219  502 QERERRLQ 509
Cdd:PRK04863  1071 ANRSRRNQ 1078
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
293-488 3.01e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  293 NATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEI 372
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  373 QISMRQEMELAMKMLEKDVCEKQDALVSLRQQ---------------LDDLRALKHELAfKLQSSDLgVKQKSELNSRLE 437
Cdd:COG4913    764 ERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALLD-RLEEDGL-PEYEERFKELLN 841

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953291219  438 EKTNQMaatIKQLEQRLRQAERG--RQSAELDNRLFKQDFGDKInSLQLEVEE 488
Cdd:COG4913    842 ENSIEF---VADLLSKLRRAIREikERIDPLNDSLKRIPFGPGR-YLRLEARP 890
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 569-614 3.30e-03

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 36.38  E-value: 3.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1953291219 569 CQLCQEDGS--LTKNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPC 614
Cdd:cd15726    10 CLDCKSEFSwmVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
 556-618 3.32e-03

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 36.56  E-value: 3.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953291219 556 GQDQP---PPSEKPQiCQLCQEDGSLTK--NVCKNCRGTFCNACSTNELPLPS-SIKPERVCNPCHEHL 618
Cdd:cd15729     1 GKVAPvwvPDSEAPN-CMQCEVKFTFTKrrHHCRACGKVLCSACCSLKARLEYlDNKEARVCVPCYQTL 68
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 292-497 3.51e-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: 40.54  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  292 LNATVNNLQAKVDALEKSNTKLTEELAVANNRiitLQEEMERVKEGPKQDRTSEGQaLSEARKHLKEETQLRLDVEK--- 368
Cdd:pfam01576  220 LQEQIAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQ-ISELQEDLESERAARNKAEKqrr 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  369 ----ELE--------------IQISMRQEMELAMKMLEKDVCEKQDalvSLRQQLDDLRAlKHELAFKLQSSDLGVKQKS 430
Cdd:pfam01576  296 dlgeELEalkteledtldttaAQQELRSKREQEVTELKKALEEETR---SHEAQLQEMRQ-KHTQALEELTEQLEQAKRN 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  431 ELN-----SRLEEKTNQMAATIKQLEQRLRQAERGR-----QSAELDNRL-----FKQDFGDKINSLQLEVEELTRQRHQ 495
Cdd:pfam01576  372 KANlekakQALESENAELQAELRTLQQAKQDSEHKRkklegQLQELQARLseserQRAELAEKLSKLQSELESVSSLLNE 451


                   ..
gi 1953291219  496 LE 497
Cdd:pfam01576  452 AE 453
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
327-510 3.70e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  327 LQEEMERVKEgpKQDrtsegqALSEARKHLKEETQLRLDVEkELEIQISMRQ--EMELAMKMLEKDVCEKQDALVSLRQQ 404
Cdd:COG4913    240 AHEALEDARE--QIE------LLEPIRELAERYAAARERLA-ELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAE 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  405 LDDLRALKHEL-----AFKLQSSDLGVKQKSELNSRLEEKTNQmaatIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKI 479
Cdd:COG4913    311 LERLEARLDALreeldELEAQIRGNGGDRLEQLEREIERLERE----LEERERRRARLEALLAALGLPLPASAEEFAALR 386

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1953291219  480 NSLQLEVEELTRQRHQLELELkQERERRLQN 510
Cdd:COG4913    387 AEAAALLEALEEELEALEEAL-AEAEAALRD 416
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 294-506 4.79e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.19  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 294 ATVNNLQAKVDALEKSNTKLTEELavanNRIITLQEEMERVKEGPKQDRTSEGQALSEAR--KHLKEETQL--------- 362
Cdd:pfam10174 192 MQLGHLEVLLDQKEKENIHLREEL----HRRNQLQPDPAKTKALQTVIEMKDTKISSLERniRDLEDEVQMlktngllht 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 363 --RLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDL-----------RALKHELAFKLQSSDLGVKQK 429
Cdd:pfam10174 268 edREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLtnqnsdckqhiEVLKESLTAKEQRAAILQTEV 347

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953291219 430 SELNSRLEEKTNQMAATIKQLeQRLrQAERGRQSAELDNRLFKQDFGD-KINSLQLEVEELTRQRHQLELELKQERER 506
Cdd:pfam10174 348 DALRLRLEEKESFLNKKTKQL-QDL-TEEKSTLAGEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLKER 423
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
294-514 5.11e-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: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  294 ATVNNLQAKVDALEKSNTKLTEelavannriitLQEEMERVKEgpkqdrtsegqALSEARKHLKEETQLRLDVEKELEiq 373
Cdd:COG4913    668 REIAELEAELERLDASSDDLAA-----------LEEQLEELEA-----------ELEELEEELDELKGEIGRLEKELE-- 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  374 iSMRQEMELAMKMLEKDVcekQDALVSLRQQLDDLRAlkhELAFKLQSSDLgvkqKSELNSRLEEKTNQMAATIKQLEQR 453
Cdd:COG4913    724 -QAEEELDELQDRLEAAE---DLARLELRALLEERFA---AALGDAVEREL----RENLEERIDALRARLNRAEEELERA 792

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953291219  454 LRQaergrqsaeldnrlFKQDFGDKINSLQLEVEELT---RQRHQLE---LELKQERERRLQNNRSI 514
Cdd:COG4913    793 MRA--------------FNREWPAETADLDADLESLPeylALLDRLEedgLPEYEERFKELLNENSI 845
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
432-527 5.18e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 432 LNSRLEEKTNQMAATIKQLEQRLRQAErgRQSAELDNRL--FKQ-----DFGDKINSLQLEVEELTRQRHQLELELKQER 504
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQLPELR--KELEEAEAALeeFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAE 239

                          90       100
                  ....*....|....*....|...
gi 1953291219 505 ERRLQNNRSIPGKGSQKPEPKTD 527
Cdd:COG3206   240 ARLAALRAQLGSGPDALPELLQS 262
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 285-545 5.23e-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: 5.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  285 VEELNRHLNATVNNLQAKVDALEKSNTKLTEELavannriitlQEEMERVKEGpKQDRTSEGQALSEARKHLKEE----T 360
Cdd:pfam01576  329 VTELKKALEEETRSHEAQLQEMRQKHTQALEEL----------TEQLEQAKRN-KANLEKAKQALESENAELQAElrtlQ 397

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  361 QLRLDVE---KELEIQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDlgvKQKSELNSRLE 437
Cdd:pfam01576  398 QAKQDSEhkrKKLEGQL---QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS---KDVSSLESQLQ 471

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219  438 EKTNQMAATIKQ---LEQRLRQAERGRQSaeLDNRL-----FKQDFGDKINSLQLEVEELTRQRHQ--LELELKQERERR 507
Cdd:pfam01576  472 DTQELLQEETRQklnLSTRLRQLEDERNS--LQEQLeeeeeAKRNVERQLSTLQAQLSDMKKKLEEdaGTLEALEEGKKR 549

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1953291219  508 LQnnRSIPGKgSQKPEPKTDGKHKIQEENVKLKKPLDE 545
Cdd:pfam01576  550 LQ--RELEAL-TQQLEEKAAAYDKLEKTKNRLQQELDD 584
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 272-445 6.09e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 272 DGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAvanNRIITLQEE--------------------- 330
Cdd:COG3883    43 QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG---ERARALYRSggsvsyldvllgsesfsdfld 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 331 -MERVKEGPKQDRtsegQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLR 409
Cdd:COG3883   120 rLSALSKIADADA----DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1953291219 410 ALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAA 445
Cdd:COG3883   196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 296-503 6.25e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.56  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 296 VNNLQAKVDALEKSNTKLTEELAVANNriiTLQEEMERVKEGPKQDRTSEGQALSEARKHlKEETQLRLDVEKELEIQIS 375
Cdd:COG5185   324 EQELEESKRETETGIQNLTAEIEQGQE---SLTENLEAIKEEIENIVGEVELSKSSEELD-SFKDTIESTKESLDEIPQN 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 376 MRQEMELA-------MKMLEKDVCEKQDALVSLRQQLDD----LRALKHELAFKLQSSDLGVKQK-----SELNSRLEEK 439
Cdd:COG5185   400 QRGYAQEIlatledtLKAADRQIEELQRQIEQATSSNEEvsklLNELISELNKVMREADEESQSRleeayDEINRSVRSK 479

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953291219 440 TNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELELKQE 503
Cdd:COG5185   480 KEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEN 543
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 296-509 6.35e-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: 39.73  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 296 VNNLQAKVDALEKSNTKL-------TEELAVANNRIITLQEEMERVKEgpkqDRTSEGQALSEARKHLKEETQLRLDVEK 368
Cdd:pfam07111 164 LSSLTSKAEGLEKSLNSLetkrageAKQLAEAQKEAELLRKQLSKTQE----ELEAQVTLVESLRKYVGEQVPPEVHSQT 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 369 -ELEiqismRQEMELAMKMLEKDVCEKQDALVSLR---QQLDDLRALKHE-LAFKLQSSDL----GVKQKSELNSRLEEK 439
Cdd:pfam07111 240 wELE-----RQELLDTMQHLQEDRADLQATVELLQvrvQSLTHMLALQEEeLTRKIQPSDSlepeFPKKCRSLLNRWREK 314

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953291219 440 TNQMAATIK--QLEQRLRQAERGRQSAELDNRLFKQDFGDKI-------NSLQLEVEELTRQRHQLELELKQERERRLQ 509
Cdd:pfam07111 315 VFALMVQLKaqDLEHRDSVKQLRGQVAELQEQVTSQSQEQAIlqralqdKAAEVEVERMSAKGLQMELSRAQEARRRQQ 393
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 286-502 6.43e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 286 EELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEgpKQDRTSEgqALSEARKHLKEETQLRLD 365
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD--EQNKIKK--QLSEKQKELEQNNKKIKE 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 366 VEKEL-----EIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELafKLQSSDLGvKQKSELNSRLEEKT 440
Cdd:TIGR04523 286 LEKQLnqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL--NEQISQLK-KELTNSESENSEKQ 362

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953291219 441 NQMAATIKQLEQRLRQAERGRQSaeldnrlfKQDFGDKINSLQLEVEELTRQRHQLELELKQ 502
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQE--------IKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
46 PHA02562
endonuclease subunit; Provisional
 281-488 7.91e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 281 QKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMErvkegpkqDRTSEGQALSEARKHLKEET 360
Cdd:PHA02562  200 YNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE--------DPSAALNKLNTAAAKIKSKI 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 361 QLrldVEKEleiqismrqemelaMKMLEK-DVC---------------EKQDALVSLRQQLDDLRALKHELAFKLQSSDL 424
Cdd:PHA02562  272 EQ---FQKV--------------IKMYEKgGVCptctqqisegpdritKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE 334

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953291219 425 GVKQKSELNSRLEEKTNQMAATIKQLE------QRLrQAERGRQSAELDnrLFKQDFGDKINSLQLEVEE 488
Cdd:PHA02562  335 QSKKLLELKNKISTNKQSLITLVDKAKkvkaaiEEL-QAEFVDNAEELA--KLQDELDKIVKTKSELVKE 401
 
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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