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Conserved domains on  [gi|2077802608|ref|XP_042653006|]
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protein RUFY3 isoform X1 [Tyto alba]

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; ...
139-294 1.52e-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: 305.00  E-value: 1.52e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 139 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 218
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 219 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 294
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
637-686 1.46e-21

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: 88.24  E-value: 1.46e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077802608 637 ICQLCQEEG-SRTKKKNVCKNCGGIFCEACSRNELPLPSSI-NPERVCNPCH 686
Cdd:cd15744     1 SCSLCQEDFaSLALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
343-644 1.70e-12

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 71.25  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  343 RHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnrkvTKDRTADGHALTEARKQLKEE 422
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-----------IGEIEKEIEQLEQEEEKLKER 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  423 -TQLRLDVeKELEVQIgmrQEMELAMKMLEKDVCEKQDALVALRQQLDDLRA-LKHElsfklqssdmGVKQKSELNSRLE 500
Cdd:TIGR02169  739 lEELEEDL-SSLEQEI---ENVKSELKELEARIEELEEDLHKLEEALNDLEArLSHS----------RIPEIQAELSKLE 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  501 EKTNQMAATIKQLEQRLQR-------AEKDRQLAQQDNRLFK---QEFGDKINSLQLEVEELSRQRSHLELE-------- 562
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAAlrdlesrl 884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  563 --LKRERDRwSHSHQRSQENKKGTKNWLRQDGKLRIQEENTNvKQPPREENSVLPHKVPSGTQEEQEQLSGPGNTKICQL 640
Cdd:TIGR02169  885 gdLKKERDE-LEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR 962

                   ....
gi 2077802608  641 CQEE 644
Cdd:TIGR02169  963 VEEE 966
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
139-294 1.52e-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: 305.00  E-value: 1.52e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 139 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 218
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 219 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 294
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
174-297 4.94e-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: 154.36  E-value: 4.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 174 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 244
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 245 KKLSEYMKALINRKDLLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 297
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
637-686 1.46e-21

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: 88.24  E-value: 1.46e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077802608 637 ICQLCQEEG-SRTKKKNVCKNCGGIFCEACSRNELPLPSSI-NPERVCNPCH 686
Cdd:cd15744     1 SCSLCQEDFaSLALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
234-296 8.96e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 77.65  E-value: 8.96e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077802608  234 GRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 296
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
636-689 1.06e-12

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: 63.61  E-value: 1.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608  636 KICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSIN--PERVCNPCHKRL 689
Cdd:smart00064  11 SNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIerPVRVCDDCYENL 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
343-644 1.70e-12

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: 71.25  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  343 RHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnrkvTKDRTADGHALTEARKQLKEE 422
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-----------IGEIEKEIEQLEQEEEKLKER 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  423 -TQLRLDVeKELEVQIgmrQEMELAMKMLEKDVCEKQDALVALRQQLDDLRA-LKHElsfklqssdmGVKQKSELNSRLE 500
Cdd:TIGR02169  739 lEELEEDL-SSLEQEI---ENVKSELKELEARIEELEEDLHKLEEALNDLEArLSHS----------RIPEIQAELSKLE 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  501 EKTNQMAATIKQLEQRLQR-------AEKDRQLAQQDNRLFK---QEFGDKINSLQLEVEELSRQRSHLELE-------- 562
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAAlrdlesrl 884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  563 --LKRERDRwSHSHQRSQENKKGTKNWLRQDGKLRIQEENTNvKQPPREENSVLPHKVPSGTQEEQEQLSGPGNTKICQL 640
Cdd:TIGR02169  885 gdLKKERDE-LEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR 962

                   ....
gi 2077802608  641 CQEE 644
Cdd:TIGR02169  963 VEEE 966
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
636-689 5.52e-11

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: 58.55  E-value: 5.52e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 636 KICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSI---NPERVCNPCHKRL 689
Cdd:pfam01363  10 TVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTL 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
327-591 2.61e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 327 QITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRT 406
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 407 ADGHALTEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSD 486
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 487 MG-VKQKSELNSRLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKR 565
Cdd:COG1196   393 RAaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                         250       260
                  ....*....|....*....|....*.
gi 2077802608 566 ERDRWSHSHQRSQENKKGTKNWLRQD 591
Cdd:COG1196   473 ALLEAALAELLEELAEAAARLLLLLE 498
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
339-565 2.60e-07

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: 54.07  E-value: 2.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  339 EELNRHLSATVNNLQAKVDALEKsntkLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQ 418
Cdd:pfam12128  600 EELRERLDKAEEALQSAREKQAA----AEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAE 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  419 LKEETQLRL-DVEKELEV---------QIGMRQEMELAMKMLEKD---VCEKQDALVALRQQLDDLRAlkhelSFKLQSS 485
Cdd:pfam12128  676 RKDSANERLnSLEAQLKQldkkhqawlEEQKEQKREARTEKQAYWqvvEGALDAQLALLKAAIAARRS-----GAKAELK 750
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  486 DMGVKQKSELNSRL--EEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELEL 563
Cdd:pfam12128  751 ALETWYKRDLASLGvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQL 830

                   ..
gi 2077802608  564 KR 565
Cdd:pfam12128  831 AR 832
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
335-582 1.07e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 335 KNYVEELNRHLSATvNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVK------EESSYILESNRKVTKDRTAD 408
Cdd:PRK03918  175 KRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevkelEELKEEIEELEKELESLEGS 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 409 GHALTEARKQLK---EETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSS 485
Cdd:PRK03918  254 KRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 486 DMGVKQKSELNSRLEEKTNQMAAtikqLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKR 565
Cdd:PRK03918  334 EEKEERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409
                         250
                  ....*....|....*..
gi 2077802608 566 ERDRWSHSHQRSQENKK 582
Cdd:PRK03918  410 ITARIGELKKEIKELKK 426
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
139-294 1.52e-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: 305.00  E-value: 1.52e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 139 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 218
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 219 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 294
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
139-294 8.65e-98

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


Pssm-ID: 439057  Cd Length: 156  Bit Score: 297.66  E-value: 8.65e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 139 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 218
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 219 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 294
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
139-293 2.62e-94

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: 288.70  E-value: 2.62e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 139 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 218
Cdd:cd17681     1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077802608 219 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 293
Cdd:cd17681    81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
139-294 5.53e-93

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: 285.26  E-value: 5.53e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 139 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 218
Cdd:cd17694     1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 219 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 294
Cdd:cd17694    81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
174-297 4.94e-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: 154.36  E-value: 4.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 174 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 244
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 245 KKLSEYMKALINRKDLLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 297
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
142-293 7.20e-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: 132.14  E-value: 7.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 142 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLG--QNKSFWGPLELVEKLVPEAAeiTA 219
Cdd:cd17684     1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 220 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 293
Cdd:cd17684    77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
150-293 1.92e-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: 122.92  E-value: 1.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 150 SIKGLIESALNLGR-------TLDSDYAPLQQFFVVMEHCLKHGLKAKKtFLGQNKSFWGPLELVEKLVPEAAEITA--S 220
Cdd:cd17671     2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKQAirD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 221 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANF 293
Cdd:cd17671    81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
142-294 4.85e-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: 104.28  E-value: 4.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 142 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQN--KSFWGPLELVEKLVPEAAeiTA 219
Cdd:cd17700     1 NLITVCRFSVKTLIDRSCF--ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHNC--IC 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077802608 220 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 294
Cdd:cd17700    77 SIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
142-294 1.91e-23

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


Pssm-ID: 439061  Cd Length: 151  Bit Score: 97.02  E-value: 1.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 142 NLMNMAKLSIKGLIESALnlGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQnKSFWGPLELVEKLVPEaaEIT 218
Cdd:cd17699     1 NLITVCRFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVPN--NCI 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 219 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 294
Cdd:cd17699    76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
637-686 1.46e-21

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: 88.24  E-value: 1.46e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077802608 637 ICQLCQEEG-SRTKKKNVCKNCGGIFCEACSRNELPLPSSI-NPERVCNPCH 686
Cdd:cd15744     1 SCSLCQEDFaSLALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
633-686 2.21e-19

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: 82.05  E-value: 2.21e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 633 GNTKICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSINPERVCNPCH 686
Cdd:cd15721     5 KEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
RUN smart00593
domain involved in Ras-like GTPase signaling;
234-296 8.96e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 77.65  E-value: 8.96e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077802608  234 GRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 296
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
638-696 3.50e-17

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: 76.22  E-value: 3.50e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSINPERVCNPCHKRLIQQYSTS 696
Cdd:cd15759    13 CKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
151-290 6.52e-17

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


Pssm-ID: 439044  Cd Length: 150  Bit Score: 78.04  E-value: 6.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 151 IKGLIESALNLGRTLDSDYAP-LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLE-LVEKLVPEA---AEITASVKDLP 225
Cdd:cd17682     2 LKGCVLDLKSEFGEITDPDNPyLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 226 GLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEE-GAIIAGLLVGLNVID 290
Cdd:cd17682    82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEIlSEILLSLLYQLNEIN 147
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
638-694 9.28e-17

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: 75.10  E-value: 9.28e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSINPERVCNPCHKRLIQQYS 694
Cdd:cd15758    15 CKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
140-286 1.65e-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: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 140 RMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAK-----KTFLGQN------KSFWGPLELV- 207
Cdd:cd17679     1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKfiskvSSVFSGDvdklpePNFWPLLLKFs 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 208 EKlvpeaaEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGL 286
Cdd:cd17679    81 HR------DVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGL 154
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
638-686 4.34e-13

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: 64.09  E-value: 4.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSIN--PERVCNPCH 686
Cdd:cd00065     2 CMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSgkPVRVCDSCY 52
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
636-689 1.06e-12

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: 63.61  E-value: 1.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608  636 KICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSIN--PERVCNPCHKRL 689
Cdd:smart00064  11 SNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIerPVRVCDDCYENL 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
343-644 1.70e-12

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: 71.25  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  343 RHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnrkvTKDRTADGHALTEARKQLKEE 422
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-----------IGEIEKEIEQLEQEEEKLKER 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  423 -TQLRLDVeKELEVQIgmrQEMELAMKMLEKDVCEKQDALVALRQQLDDLRA-LKHElsfklqssdmGVKQKSELNSRLE 500
Cdd:TIGR02169  739 lEELEEDL-SSLEQEI---ENVKSELKELEARIEELEEDLHKLEEALNDLEArLSHS----------RIPEIQAELSKLE 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  501 EKTNQMAATIKQLEQRLQR-------AEKDRQLAQQDNRLFK---QEFGDKINSLQLEVEELSRQRSHLELE-------- 562
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAAlrdlesrl 884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  563 --LKRERDRwSHSHQRSQENKKGTKNWLRQDGKLRIQEENTNvKQPPREENSVLPHKVPSGTQEEQEQLSGPGNTKICQL 640
Cdd:TIGR02169  885 gdLKKERDE-LEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR 962

                   ....
gi 2077802608  641 CQEE 644
Cdd:TIGR02169  963 VEEE 966
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
224-289 4.02e-12

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


Pssm-ID: 439051  Cd Length: 166  Bit Score: 64.94  E-value: 4.02e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 224 LPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVI 289
Cdd:cd17689    93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-579 6.51e-12

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: 69.32  E-value: 6.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  314 KDGNSTKGSegDGQITAILDQKNYVEELNRH---LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 390
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  391 SSYILESNRKVTKDRTADGHALTEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDD 470
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  471 LRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQL-----EQRLQRAEKDRQLAQQDNRLFKQEFG-----D 540
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeieELEELIEELESELEALLNERASLEEAlallrS 894
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2077802608  541 KINSLQLEVEELSRQRSHLELELKRERDRWSHSHQRSQE 579
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
636-689 5.52e-11

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: 58.55  E-value: 5.52e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 636 KICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSI---NPERVCNPCHKRL 689
Cdd:pfam01363  10 TVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTL 66
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
634-686 6.80e-11

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: 57.92  E-value: 6.80e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077802608 634 NTKICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLP--SSINPERVCNPCH 686
Cdd:cd15735     5 DSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
180-290 7.36e-11

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: 61.15  E-value: 7.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 180 EHCLKHGLKAKK-TFLGQNKSFwGPLELVEKLVPEAAEITASVKDL------PGLKTPVGRGRA-------------WLR 239
Cdd:cd17687    31 DACLLHGLRKRAlGLFRSSSTF-SLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIR 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077802608 240 LALMQKKLSEYMKALINRKdllSEFYEPNALMME-EEGAIIAGLLVGLNVID 290
Cdd:cd17687   110 IALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
179-289 9.88e-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: 60.58  E-value: 9.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 179 MEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRK 258
Cdd:cd17697    35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2077802608 259 DLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVI 289
Cdd:cd17697   115 ELTGEWYYARSpFLSPELRSDILDSLYELNGV 146
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
638-689 1.84e-10

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: 57.02  E-value: 1.84e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSINPERVCNPCHKRL 689
Cdd:cd15730    12 CMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL 63
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
150-271 2.31e-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: 59.18  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 150 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKktflgqNKSFWGpleLVEKLVPEAAEItaSVKDLPGLKT 229
Cdd:cd17680    12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRG------NRGYWP---FVKEFTHKETIK--QIENLPNVTT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2077802608 230 PVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALM 271
Cdd:cd17680    81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
327-591 2.61e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 327 QITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRT 406
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 407 ADGHALTEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSD 486
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 487 MG-VKQKSELNSRLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKR 565
Cdd:COG1196   393 RAaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                         250       260
                  ....*....|....*....|....*.
gi 2077802608 566 ERDRWSHSHQRSQENKKGTKNWLRQD 591
Cdd:COG1196   473 ALLEAALAELLEELAEAAARLLLLLE 498
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
638-689 2.65e-10

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: 56.63  E-value: 2.65e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPS--SINPERVCNPCHKRL 689
Cdd:cd15719    12 CTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
638-685 1.51e-09

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: 54.27  E-value: 1.51e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSI--NPERVCNPC 685
Cdd:cd15731    14 CMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
145-293 1.62e-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: 57.01  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 145 NMAKLSIKGLIESALNLGRTLDSDYAP-------LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEI 217
Cdd:cd17698     2 SQLQKIIRDLQDCVTELKKEFEETGEPitddsttLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLNDG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 218 TASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEP-NALMMEEEGAIIAGLLVGLNviDANF 293
Cdd:cd17698    82 IRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPrSVFLNHKYSSDIINSLYDLN--EVQF 156
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
185-294 1.69e-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: 57.79  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 185 HGLKAKktflgQNKS-FWGPL----ELVEKLVPEAAEITA---SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALIN 256
Cdd:cd17677    65 HGLQTK-----QGKSaLWSHLlayqENEERLKPLPESLLFdmkNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2077802608 257 RKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 294
Cdd:cd17677   140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVDY-FC 177
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
638-686 2.53e-09

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: 53.59  E-value: 2.53e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSS--INPERVCNPCH 686
Cdd:cd15733    10 CFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEqlYDPVRVCNSCY 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
335-560 3.30e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 3.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  335 KNYVEELNRHLSAtVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTE 414
Cdd:TIGR02168  263 QELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  415 ARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSD-------- 486
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrerlqq 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  487 --------MGVKQKSELNSRLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFkQEFGDKINSLQLEVEELSRQRSH 558
Cdd:TIGR02168  422 eieellkkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQEN 500

                   ..
gi 2077802608  559 LE 560
Cdd:TIGR02168  501 LE 502
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
638-685 4.07e-09

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: 53.11  E-value: 4.07e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSS--INPERVCNPC 685
Cdd:cd15734    11 CSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
638-689 4.86e-09

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: 52.77  E-value: 4.86e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPS-SINPE-RVCNPCHKRL 689
Cdd:cd15720     8 CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKfGIEKEvRVCDPCYEKL 61
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
318-569 5.23e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 5.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  318 STKGSEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE---SSYI 394
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkaLREA 804
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  395 LESNRKVTKDRTADGHALTEARKQLKEETQlrlDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRAL 474
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIA---ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  475 K-------HELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLQRAEKDR-QLAQQDNRLFKQEFGDKINSLQ 546
Cdd:TIGR02168  882 RasleealALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEALEN 961
                          250       260
                   ....*....|....*....|...
gi 2077802608  547 LEVEELSRQRSHLElELKRERDR 569
Cdd:TIGR02168  962 KIEDDEEEARRRLK-RLENKIKE 983
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
638-685 7.23e-09

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: 52.38  E-value: 7.23e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLP--SSINPERVCNPC 685
Cdd:cd15727    13 CMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
637-685 1.37e-08

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: 51.35  E-value: 1.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077802608 637 ICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSINP--ERVCNPC 685
Cdd:cd15745     1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCiyLRVCKTC 51
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
638-685 1.45e-08

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: 51.44  E-value: 1.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSS--INPERVCNPC 685
Cdd:cd15732    11 CYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQqlFEPSRVCKSC 60
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
638-691 1.58e-08

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: 51.96  E-value: 1.58e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSINPERVCNPCHKRLIQ 691
Cdd:cd15739    13 CPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
172-292 1.90e-08

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: 53.81  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 172 LQQFFVVMEHCLKHGLKAKKTFLGQNkSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVG-RGRAWLRLALMQKKLSEY 250
Cdd:cd17686    21 LQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGRLWLRQSLQQHCLSSQ 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2077802608 251 MKALINRKDLLSEFYEPNALMMEEEGAiiAGLLVGLNVIDAN 292
Cdd:cd17686   100 LQWLVSDKELLRKYYEDEAFLRQEGYA--TALLICLTAVELN 139
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
638-686 2.81e-08

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: 50.76  E-value: 2.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSI---NPERVCNPCH 686
Cdd:cd15760     8 CDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
339-579 4.77e-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: 4.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 339 EELNRhLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnrkvtkdRTADGHALTEARKQ 418
Cdd:COG1196   281 LELEE-AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE--------------LEELEEELEELEEE 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 419 LKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSsdmgvkQKSELNSR 498
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA------LLERLERL 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 499 LEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKRERDRWSHSHQRSQ 578
Cdd:COG1196   420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499

                  .
gi 2077802608 579 E 579
Cdd:COG1196   500 E 500
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
221-294 8.13e-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: 53.14  E-value: 8.13e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077802608 221 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 294
Cdd:cd17691   127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVDY-FC 200
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
319-508 2.10e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.68  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 319 TKGSEGDGQITAILDQKNYVE-ELNRhLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE------S 391
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQaELDA-LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerarA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 392 SY-----------ILESN---------RKVTKDRTADGHALTEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLE 451
Cdd:COG3883    95 LYrsggsvsyldvLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 452 KDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAA 508
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
339-565 2.60e-07

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: 54.07  E-value: 2.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  339 EELNRHLSATVNNLQAKVDALEKsntkLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQ 418
Cdd:pfam12128  600 EELRERLDKAEEALQSAREKQAA----AEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAE 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  419 LKEETQLRL-DVEKELEV---------QIGMRQEMELAMKMLEKD---VCEKQDALVALRQQLDDLRAlkhelSFKLQSS 485
Cdd:pfam12128  676 RKDSANERLnSLEAQLKQldkkhqawlEEQKEQKREARTEKQAYWqvvEGALDAQLALLKAAIAARRS-----GAKAELK 750
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  486 DMGVKQKSELNSRL--EEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELEL 563
Cdd:pfam12128  751 ALETWYKRDLASLGvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQL 830

                   ..
gi 2077802608  564 KR 565
Cdd:pfam12128  831 AR 832
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
412-599 4.50e-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: 53.42  E-value: 4.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  412 LTEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDV--CEKQDALVALRQQLDDLRALKHelsfklqssdmgv 489
Cdd:COG3096    443 LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWQTARELLRRYRSQQA------------- 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  490 kqkselnsrLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINsLQLEVEELSRQRSHLELELKRERDR 569
Cdd:COG3096    510 ---------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEAQLEELEEQAAEAVEQ 579
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2077802608  570 WSHSHQ-------RSQENKKGTKNWLRQDGKL-RIQEE 599
Cdd:COG3096    580 RSELRQqleqlraRIKELAARAPAWLAAQDALeRLREQ 617
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
326-569 4.92e-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: 4.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 326 GQITAILDQKNYVEELNRHLSAtvnnLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKVTKDR 405
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 406 TAdghALTEARKQLKEETQLRLDV----EKELEVQIGMRQE----MELAMKMLEKDVCEKQDALVALRQQLDDLRALKHE 477
Cdd:COG4942    92 IA---ELRAELEAQKEELAELLRAlyrlGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 478 LSFKLQssdmgvkQKSELNSRLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQdnrlfkqefgdKINSLQLEVEELSRQRS 557
Cdd:COG4942   169 LEAERA-------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAA-----------ELAELQQEAEELEALIA 230
                         250
                  ....*....|..
gi 2077802608 558 HLELELKRERDR 569
Cdd:COG4942   231 RLEAEAAAAAER 242
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
635-689 5.53e-07

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, 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.


Pssm-ID: 277293 [Multi-domain]  Cd Length: 64  Bit Score: 47.26  E-value: 5.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 635 TKICQLC-QEEGSRTKKKNVCKNCGGIFCEACSRNELPLPS-SINPERVCNPCHKRL 689
Cdd:cd15754     8 TDICMRCtQTNFSLLTRRHHCRKCGFVVCHECSRQRFLIPRlSPKPVRVCSLCYRKL 64
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
638-686 8.40e-07

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: 46.34  E-value: 8.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSIN-PERVCNPCH 686
Cdd:cd15749     2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRKGNqKQKVCKQCH 51
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
638-685 1.37e-06

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: 46.01  E-value: 1.37e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSINPERVCNPC 685
Cdd:cd15726    10 CLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
339-627 1.46e-06

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: 51.56  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 339 EELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQ 418
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 419 LKE--------ETQLRLDVEKELEVQIGMRQ------------------EMELAMKMLEKDVCEKQDALVALRQQL---- 468
Cdd:TIGR04523 290 LNQlkseisdlNNQKEQDWNKELKSELKNQEkkleeiqnqisqnnkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 469 DDLRALKHELSFKLQSSDMGVKQKSELNSRL---EEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGD---KI 542
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIqnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDltnQD 449
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 543 NSLQLEVEELSRQRSHLELELKrerdrwshSHQRSQENKKGTKNWLRQDGKLRIQEEN--TNVKQPPREENSVLPHKVPS 620
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLK--------VLSRSINKIKQNLEQKQKELKSKEKELKklNEEKKELEEKVKDLTKKISS 521

                  ....*..
gi 2077802608 621 GTQEEQE 627
Cdd:TIGR04523 522 LKEKIEK 528
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
353-569 1.62e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  353 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESsyilesnrkvtkdrtadghaltEARKQLKEETQLRLDVEkE 432
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR----------------------EALQRLAEYSWDEIDVA-S 665
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  433 LEVQIgmrQEMELAMKMLEKDvcekQDALVALRQQLDDLRALKHELSFKLqssdmgvKQKSELNSRLEEKTNQMAATIKQ 512
Cdd:COG4913    666 AEREI---AELEAELERLDAS----SDDLAALEEQLEELEAELEELEEEL-------DELKGEIGRLEKELEQAEEELDE 731
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2077802608  513 LEQRLQRAEKDRQLAQQDN--RLFKQEFGDkiNSLQLEVEELSRQRSHLELELKRERDR 569
Cdd:COG4913    732 LQDRLEAAEDLARLELRALleERFAAALGD--AVERELRENLEERIDALRARLNRAEEE 788
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
369-582 2.21e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 369 ELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQLKEETQL--------------RLDVEKELE 434
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaqaeeyellaeLARLEQDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 435 VQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLE 514
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077802608 515 QRLQRAEKDR-QLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKRERDRWSHSHQRSQENKK 582
Cdd:COG1196   386 EELLEALRAAaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
RUN_SGSM1 cd17703
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ...
151-285 2.45e-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: 48.47  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 151 IKGLIESALNLgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKT-FLGQNK----------SFWGPLELVEKL--------- 210
Cdd:cd17703     3 VKQIMEEAVTR-KFVHEDSSHIISFCAAVEACVLHGLKRRAAgFLRSNKiaalfmkvgkSFPPAEELCRKVqeleqllen 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 211 ----VPEAAEITASVKDLPGLkTPVGRGRAWLRLALMQKKLSEYMKALINRKdllSEFYEPNALMMEE-EGAIIAGLLVG 285
Cdd:cd17703    82 krnqMQGLQENVRKMPKLPNL-SPQAIKHLWIRTALFEKVLDKIVHYLVENS---SKYYEKEALLMDPvDGPILASLLVG 157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
339-560 2.51e-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: 51.22  E-value: 2.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  339 EELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTAdghaLTEARKQ 418
Cdd:TIGR02169  286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK----LTEEYAE 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  419 LKEETQ-LRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELNS 497
Cdd:TIGR02169  362 LKEELEdLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608  498 RLEEKtnqmAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFG---DKINSLQLEVEELSRQRSHLE 560
Cdd:TIGR02169  442 EKEDK----ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDrveKELSKLQRELAEAEAQARASE 503
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
350-566 4.82e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 350 NNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI-LESNRKVTKDRtadghaLTEARKQLkEETQLRLd 428
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVdLSEEAKLLLQQ------LSELESQL-AEARAEL- 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 429 veKELEVQIGMRQEMeLAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVK----QKSELNSRLEEKTN 504
Cdd:COG3206   236 --AEAEARLAALRAQ-LGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIalraQIAALRAQLQQEAQ 312
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 505 QMAATIKQLEQRLQRAEKD--RQLAQQDNRLfkqefgDKINSLQLEVEELSRqrshlELELKRE 566
Cdd:COG3206   313 RILASLEAELEALQAREASlqAQLAQLEARL------AELPELEAELRRLER-----EVEVARE 365
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
637-686 5.09e-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: 5.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077802608 637 ICQLCQE-EGSRTKKKNVCKNCGGIFCEACSRNELPLPS-SINPERVCNPCH 686
Cdd:cd15717    10 VCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
637-685 5.19e-06

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.


Pssm-ID: 277282 [Multi-domain]  Cd Length: 61  Bit Score: 44.35  E-value: 5.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077802608 637 ICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSIN-PERVCNPC 685
Cdd:cd15743    11 MCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLKNkSARVCDEC 60
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
637-689 7.62e-06

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277281 [Multi-domain]  Cd Length: 67  Bit Score: 44.15  E-value: 7.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 637 ICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPS-SINPERVCNPCHKRL 689
Cdd:cd15742    11 MCMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPLKYlKDRPAKVCDGCFAEL 64
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
650-686 8.45e-06

FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277277 [Multi-domain]  Cd Length: 61  Bit Score: 43.86  E-value: 8.45e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2077802608 650 KKNVCKNCGGIFCEACSRNELPLPS--SINPERVCNPCH 686
Cdd:cd15738    23 KKHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
335-582 1.07e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 335 KNYVEELNRHLSATvNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVK------EESSYILESNRKVTKDRTAD 408
Cdd:PRK03918  175 KRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevkelEELKEEIEELEKELESLEGS 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 409 GHALTEARKQLK---EETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSS 485
Cdd:PRK03918  254 KRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 486 DMGVKQKSELNSRLEEKTNQMAAtikqLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKR 565
Cdd:PRK03918  334 EEKEERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409
                         250
                  ....*....|....*..
gi 2077802608 566 ERDRWSHSHQRSQENKK 582
Cdd:PRK03918  410 ITARIGELKKEIKELKK 426
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
637-685 1.12e-05

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 43.57  E-value: 1.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077802608 637 ICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELP-LPSSIN-PERVCNPC 685
Cdd:cd15728     9 YCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPiIKFDLNkPVRVCDVC 59
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
637-689 1.17e-05

FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, 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: 277294 [Multi-domain]  Cd Length: 64  Bit Score: 43.49  E-value: 1.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077802608 637 ICQLCQE-EGSRTKKKNVCKNCGGIFCEACSRNELPLPS-SINPERVCNPCHKRL 689
Cdd:cd15755    10 VCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
637-689 1.28e-05

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: 43.50  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 637 ICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSINPE-RVCNPCHKRL 689
Cdd:cd15729    15 NCMQCEVKFTFTKRRHHCRACGKVLCSACCSLKARLEYLDNKEaRVCVPCYQTL 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
364-579 1.46e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  364 TKLTEELAVANNRIITLQEEMERVKEessyIL-ESNRKVTK-DRTADghaLTEARKQLKEE-TQLRLDVE-KELEVQIGM 439
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLED----ILnELERQLKSlERQAE---KAERYKELKAElRELELALLvLRLEELREE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  440 RQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLQR 519
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  520 AEKDRQLAQQDnrlfKQEFGDKINSLQLEVEELSRQRSHLELELKRERDRWSHSHQRSQE 579
Cdd:TIGR02168  321 LEAQLEELESK----LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
634-687 1.55e-05

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 43.08  E-value: 1.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 634 NTKICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSINPE--RVCNPCHK 687
Cdd:cd15725     7 SCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGdlRVCTYCCK 62
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
338-569 2.86e-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: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  338 VEELNRHLSATVNNLQAKVDALEKSNTKLTEELAvANNRIITLQEEMeRVK--------EESSYILESNRKVTKDRTAdg 409
Cdd:pfam01576   17 VKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-AETELCAEAEEM-RARlaarkqelEEILHELESRLEEEEERSQ-- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  410 hALTEARKQLKEETQlrlDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGV 489
Cdd:pfam01576   93 -QLQNEKKKMQQHIQ---DLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  490 KQKSELNSRLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGD---KINSLQLEVEELSRQRSHLELELKRE 566
Cdd:pfam01576  169 AEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDlqeQIAELQAQIAELRAQLAKKEEELQAA 248

                   ...
gi 2077802608  567 RDR 569
Cdd:pfam01576  249 LAR 251
mukB PRK04863
chromosome partition protein MukB;
350-578 3.27e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.64  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  350 NNLQAKVDALEKSNTKLTEELAVANNRI------ITLQEEMERVK---EESSYILESNRKVTKDrTADGHALTEARKQLK 420
Cdd:PRK04863   310 VEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQadlEELEERLEEQNEVVEE-ADEQQEENEARAEAA 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  421 EETQLRL-----DVEKELEVQIGMRQEMELAMKMLEK-------------DVCEKQDALVALRQQLDD-LRALKHelsfK 481
Cdd:PRK04863   389 EEEVDELksqlaDYQQALDVQQTRAIQYQQAVQALERakqlcglpdltadNAEDWLEEFQAKEQEATEeLLSLEQ----K 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  482 LQSSDMGVKQKS-----------------------ELNSRLEEKTNQmAATIKQLEQRLQRAEKDRQLAQQDNRL---FK 535
Cdd:PRK04863   465 LSVAQAAHSQFEqayqlvrkiagevsrseawdvarELLRRLREQRHL-AEQLQQLRMRLSELEQRLRQQQRAERLlaeFC 543
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2077802608  536 QEFGDKINS---LQLEVEELSRQRSHLELELKRERDRWS-HSHQRSQ 578
Cdd:PRK04863   544 KRLGKNLDDedeLEQLQEELEARLESLSESVSEARERRMaLRQQLEQ 590
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
410-560 3.46e-05

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: 45.69  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 410 HALTEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLD------DLRALKHELSFklq 483
Cdd:COG1579    24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQKEIES--- 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 484 ssdmgvkQKSELnSRLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLE 560
Cdd:COG1579   101 -------LKRRI-SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
313-568 4.23e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.04  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 313 LKDGNSTKGSEGDGQITAILDQKNYVEELNRHLSATvnNLQAKVDALEKSNTkltEELAVANNRIITL-------QEEME 385
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQ---EEIAMEISRMRELerlqmerQQKNE 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 386 RVKEEssyiLESNRKVtkdRTADGHALTEARKQLKEETQLRLDVEKELEVQIG-MRQEMELAMKMLEKDVCEKQDALVAL 464
Cdd:pfam17380 393 RVRQE----LEAARKV---KILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrLEEERAREMERVRLEEQERQQQVERL 465
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 465 RQQLDDLRALKHELSFKLQSSDMGVKQK-----SELNSR----LEEKtNQMAATIKQLEQRlQRA---EKDRQLAQQDNR 532
Cdd:pfam17380 466 RQQEEERKRKKLELEKEKRDRKRAEEQRrkileKELEERkqamIEEE-RKRKLLEKEMEER-QKAiyeEERRREAEEERR 543
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2077802608 533 lfKQEFGDKINSLQLEVEELSRQRSHLElELKRERD 568
Cdd:pfam17380 544 --KQQEMEERRRIQEQMRKATEERSRLE-AMERERE 576
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
340-602 4.95e-05

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: 46.64  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 340 ELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHAL-----TE 414
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLeellrTE 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 415 ARKQLKEETQLRL---DVEK---ELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQ---QLDDLRALKHELSFKLQSS 485
Cdd:pfam05483 369 QQRLEKNEDQLKIitmELQKkssELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekIAEELKGKEQELIFLLQAR 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 486 DMGV------------------KQKSELNSRLEEK----------TNQMAATIKQLEQR-------LQRAEKD-RQLAQQ 529
Cdd:pfam05483 449 EKEIhdleiqltaiktseehylKEVEDLKTELEKEklknieltahCDKLLLENKELTQEasdmtleLKKHQEDiINCKKQ 528
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077802608 530 DNRLFKQefgdkINSLQLEVEELSRQRSHLELELKRERDRWSHSHQRSQENKKGTK-NWLRQDGKLRIQEENTN 602
Cdd:pfam05483 529 EERMLKQ-----IENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEyEVLKKEKQMKILENKCN 597
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
221-294 7.80e-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: 44.61  E-value: 7.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077802608 221 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 294
Cdd:cd17690   130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVDY-FC 203
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
327-581 8.19e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.12  E-value: 8.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  327 QITAILDQknyvEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIItLQEEMERVKEESSyilesnRKVTKDRT 406
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE-LQQRYAELCAAAI------TCTAQCEK 455
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  407 ADGHALTEARKQLKEETQLRLDVEKELEVQIGMRQEME---LAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQ 483
Cdd:TIGR00618  456 LEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  484 SSDMGVKQKSELNSRLEEKTNQmaatIKQLEQRLQRAEKDRQ-LAQQDNRLfkqefGDKINSLQLEVEELsRQRSHLELE 562
Cdd:TIGR00618  536 TYAQLETSEEDVYHQLTSERKQ----RASLKEQMQEIQQSFSiLTQCDNRS-----KEDIPNLQNITVRL-QDLTEKLSE 605
                          250
                   ....*....|....*....
gi 2077802608  563 LKRERDRWSHSHQRSQENK 581
Cdd:TIGR00618  606 AEDMLACEQHALLRKLQPE 624
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
324-603 1.05e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 324 GDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnrkvtk 403
Cdd:COG4372     1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 404 drtadghaLTEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQ 483
Cdd:COG4372    68 --------LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 484 SSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLQRAEK-------DRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQR 556
Cdd:COG4372   140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEaeaeqalDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2077802608 557 SHLELELKRERDRWSHSHQRSQENKKGTKNWLRQDGKLRIQEENTNV 603
Cdd:COG4372   220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
339-570 1.29e-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: 45.49  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  339 EELNRHLSATVNNLQA----KVDALEKSNTKLTEELAVANNRIITLQEEMERVK--EESS--YILESNRKVTKDRTADGH 410
Cdd:pfam15921  141 EDLRNQLQNTVHELEAakclKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVdfEEASgkKIYEHDSMSTMHFRSLGS 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  411 ALTEARKQLKEETQLR----LDVEKELEVQIGMRQ-EMELAMKM----LEKDVCEKQDALVALRQQLDDLRALKHELSFK 481
Cdd:pfam15921  221 AISKILRELDTEISYLkgriFPVEDQLEALKSESQnKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQ 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  482 LQ--------SSDMGVKQKSELNS-------RLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQ 546
Cdd:pfam15921  301 LEiiqeqarnQNSMYMRQLSDLEStvsqlrsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
                          250       260
                   ....*....|....*....|....
gi 2077802608  547 LEVEELSRQRSHLELELKRERDRW 570
Cdd:pfam15921  381 KLLADLHKREKELSLEKEQNKRLW 404
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
352-538 1.39e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 352 LQAKVDALEKSNtkltEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTAdgHALTEARKQLKEETQLRLDVEK 431
Cdd:COG4717    76 LEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEALEAELAELPERLE 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 432 ELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDdlRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQmaatIK 511
Cdd:COG4717   150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQEE----LE 223
                         170       180
                  ....*....|....*....|....*..
gi 2077802608 512 QLEQRLQRAEKDRQLAQQDNRLFKQEF 538
Cdd:COG4717   224 ELEEELEQLENELEAAALEERLKEARL 250
PTZ00121 PTZ00121
MAEBL; Provisional
382-599 1.74e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  382 EEMERVKEESSYIL---ESNRKVTKDRTADGHALTEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQ 458
Cdd:PTZ00121  1567 EEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  459 DALVALRQQLDDLRALKHELSFKLQSSdmgvKQKSELNSRLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNR----LF 534
Cdd:PTZ00121  1647 KKAEELKKAEEENKIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkaeeLK 1722
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077802608  535 KQEFGDKINSLQLEVEELSRQRSHLELElKRERDRWSHSHQRSQENKKGTKnwLRQDGKLRIQEE 599
Cdd:PTZ00121  1723 KAEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKEEEKKAEE--IRKEKEAVIEEE 1784
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
298-554 1.82e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  298 EDLDSQVGVIDFSMylkDGNSTKGSEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRI 377
Cdd:TIGR02168  298 SRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  378 ITLQEEMERVKEESSYILESNRKVTKDrtadghaLTEARKQLkeeTQLRLDVEKELEVQIGMRQEMELAmkmlekdvcek 457
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNE-------IERLEARL---ERLEDRRERLQQEIEELLKKLEEA----------- 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  458 qdALVALRQQLDDLRALKHELsfklqssdmgVKQKSELNSRLEEKTNQmaatIKQLEQRLQRAEkdRQLAQQDNRLfkqe 537
Cdd:TIGR02168  434 --ELKELQAELEELEEELEEL----------QEELERLEEALEELREE----LEEAEQALDAAE--RELAQLQARL---- 491
                          250
                   ....*....|....*..
gi 2077802608  538 fgDKINSLQLEVEELSR 554
Cdd:TIGR02168  492 --DSLERLQENLEGFSE 506
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
316-555 1.88e-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: 45.11  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  316 GNSTKGSEGDGQITAILDQKNYVEELNRH-----------LSATVNNLQA-----------KVDALEK----SNTKLTE- 368
Cdd:pfam15921  282 GLTEKASSARSQANSIQSQLEIIQEQARNqnsmymrqlsdLESTVSQLRSelreakrmyedKIEELEKqlvlANSELTEa 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  369 ---------ELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQLKE---ETQLRLDVEKELEVQ 436
Cdd:pfam15921  362 rterdqfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmEVQRLEALLKAMKSE 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  437 IGMRQEMELAMKMLEKDVCEKQDALVA-LRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQ 515
Cdd:pfam15921  442 CQGQMERQMAAIQGKNESLEKVSSLTAqLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK 521
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2077802608  516 RLQRAEkdrqLAQQDNRLFKQEfGDKINSLQLEVEELSRQ 555
Cdd:pfam15921  522 LRSRVD----LKLQELQHLKNE-GDHLRNVQTECEALKLQ 556
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
370-569 2.15e-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: 43.98  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 370 LAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQLKEETQLRLDVEKELevqigmrQEMELAMKM 449
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-------AALEAELAE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 450 LEKDVCEKQDALVALRQQLDD-LRAL-----KHELSFKLQSSDMGVKQKS-----ELNSRLEEKTNQMAATIKQLEQRLQ 518
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAElLRALyrlgrQPPLALLLSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRA 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2077802608 519 RAEKDRQLAQQDnrlfKQEFGDKINSLQLEVEELSRQRSHLELELKRERDR 569
Cdd:COG4942   168 ELEAERAELEAL----LAELEEERAALEALKAERQKLLARLEKELAELAAE 214
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
384-595 2.19e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 384 MERVKEESSYILESNRKVTKDRTADGHALTEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVcEKQDALVA 463
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-EKLEKLLQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 464 LRQQLDDLRALKHELSfklqssdmgvkqksELNSRLEEKTNQMAAtIKQLEQRLQRAEKDRQLAQQD----NRLFKQEFG 539
Cdd:COG4717   127 LLPLYQELEALEAELA--------------ELPERLEELEERLEE-LRELEEELEELEAELAELQEEleelLEQLSLATE 191
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 540 DKINSLQLEVEELSRQRSHLELELKRERDRwshsHQRSQENKKGTKNWLRQDGKLR 595
Cdd:COG4717   192 EELQDLAEELEELQQRLAELEEELEEAQEE----LEELEEELEQLENELEAAALEE 243
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
638-685 2.59e-04

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 39.21  E-value: 2.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077802608 638 CQLCQEE-GSRTKKKNVCKNCGGIFCEACSRNElplPSSINPERVCNPC 685
Cdd:cd15740     8 CKGCNESfNSITKRRHHCKQCGAVICGKCSEFK---DLASRHNRVCRDC 53
46 PHA02562
endonuclease subunit; Provisional
334-568 3.10e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 334 QKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMErvkeessyilesnrkvtkDRTADGHALT 413
Cdd:PHA02562  200 YNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE------------------DPSAALNKLN 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 414 EARKQLKEETQLrldVEKElevqigmrqemelaMKMLEK-DVC---------------EKQDALVALRQQLDDLRALKHE 477
Cdd:PHA02562  262 TAAAKIKSKIEQ---FQKV--------------IKMYEKgGVCptctqqisegpdritKIKDKLKELQHSLEKLDTAIDE 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 478 LSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQleqrLQRAEKDRQLAQQDNRLFKQEfgdkINSLQLEVEELSRQRS 557
Cdd:PHA02562  325 LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEE----LAKLQDELDKIVKTKS 396
                         250
                  ....*....|.
gi 2077802608 558 HLELElKRERD 568
Cdd:PHA02562  397 ELVKE-KYHRG 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
417-600 3.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 417 KQLKEETQLRldvekELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELN 496
Cdd:COG1196   216 RELKEELKEL-----EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 497 SRLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQEfgdkINSLQLEVEELSRQRSHLELELKRERDRWSHSHQR 576
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
                         170       180
                  ....*....|....*....|....
gi 2077802608 577 SQENKKGTKNWLRQDGKLRIQEEN 600
Cdd:COG1196   367 LLEAEAELAEAEEELEELAEELLE 390
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
333-569 3.23e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 333 DQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyILESNRKvtkdrtadghaL 412
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAE-----------I 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 413 TEARKQLKEetQLRldvekelEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALkhelsFKLQSSDMgvKQK 492
Cdd:COG3883    82 EERREELGE--RAR-------ALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADL-----LEELKADK--AEL 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 493 SELNSRLEEKTNQMAATIKQLEQRlqRAEKDRQLAQQDNrlfkqefgdKINSLQLEVEELSRQRSHLELELKRERDR 569
Cdd:COG3883   146 EAKKAELEAKLAELEALKAELEAA--KAELEAQQAEQEA---------LLAQLSAEEAAAEAQLAELEAELAAAEAA 211
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
383-521 3.91e-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: 43.57  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 383 EMERVKEES---SYILESNRKVTKDRTADGHAL-TEARKQLKEETQLRLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQ 458
Cdd:pfam17380 447 EMERVRLEEqerQQQVERLRQQEEERKRKKLELeKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 459 DALV--ALRQQLDDLRALKHELSFKLQSSDMgVKQKSELNSRLE--EKTNQMAATIKQLEQRLQRAE 521
Cdd:pfam17380 527 KAIYeeERRREAEEERRKQQEMEERRRIQEQ-MRKATEERSRLEamEREREMMRQIVESEKARAEYE 592
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
325-608 3.91e-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: 43.94  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 325 DGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKVTKD 404
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMS----LQRSMSTQKA 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 405 RTADGHALTEARKQLKEETqlrldvEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQL----DDLRALKHELSF 480
Cdd:pfam05483 315 LEEDLQIATKTICQLTEEK------EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLekneDQLKIITMELQK 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 481 KLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLQ--RAEKDRQLAQQDNRLFKQEFGDKINSLQLEV-------EE 551
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseEH 468
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077802608 552 LSRQRSHLELELKRER----DRWSHSHQRSQENKKGTKNWLRQDGKLRIQEE--NTNVKQPPR 608
Cdd:pfam05483 469 YLKEVEDLKTELEKEKlkniELTAHCDKLLLENKELTQEASDMTLELKKHQEdiINCKKQEER 531
PLN02939 PLN02939
transferase, transferring glycosyl groups
319-557 4.78e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 43.74  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 319 TKGSEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESN 398
Cdd:PLN02939  177 MRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETE 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 399 RKVTKdrTADGHALTEARKQlkeETQLRLDVEKELEVQIGMRQ------EMELAMKMLEKdVCEKQDALVALRQQLDDLR 472
Cdd:PLN02939  257 ERVFK--LEKERSLLDASLR---ELESKFIVAQEDVSKLSPLQydcwweKVENLQDLLDR-ATNQVEKAALVLDQNQDLR 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 473 ALKHELSFKLQSSDMgvkqkSELNSrleEKTNQMAATIKQLEQRLQRAEKDR----QLAQQDnrlfKQEFGDKINSLQLE 548
Cdd:PLN02939  331 DKVDKLEASLKEANV-----SKFSS---YKVELLQQKLKLLEERLQASDHEIhsyiQLYQES----IKEFQDTLSKLKEE 398

                  ....*....
gi 2077802608 549 VEELSRQRS 557
Cdd:PLN02939  399 SKKRSLEHP 407
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
329-569 4.89e-04

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: 43.41  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 329 TAILDQKNYVEELNRHLSAT--VNNLQAKVDALEKSNTKLTEELAVANNriiTLQEEMERVKEESSYILESNRKVTKDRT 406
Cdd:COG5185   302 TKSIDIKKATESLEEQLAAAeaEQELEESKRETETGIQNLTAEIEQGQE---SLTENLEAIKEEIENIVGEVELSKSSEE 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 407 ADGHALTEARKQLKEETQLRLDVEKELEVQIGMRQEmelaMKMLEKDVCEKQDALVALRQQLDD----LRALKHELSFKL 482
Cdd:COG5185   379 LDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDT----LKAADRQIEELQRQIEQATSSNEEvsklLNELISELNKVM 454
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 483 QSSDMGVKQK-----SELNSRLEEKTNQMAATIKQLEQRLqrAEKDRQLAQQDNRLFKQ--EFGDKINSLQLEVEELSRQ 555
Cdd:COG5185   455 READEESQSRleeayDEINRSVRSKKEDLNEELTQIESRV--STLKATLEKLRAKLERQleGVRSKLDQVAESLKDFMRA 532
                         250
                  ....*....|....
gi 2077802608 556 RSHLELELKRERDR 569
Cdd:COG5185   533 RGYAHILALENLIP 546
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
338-516 6.89e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.90  E-value: 6.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 338 VEELNRHLSATVNNL----QAKVDA---LEKSNTKLTEELAVANNRIITLQEEMERVKEesSYIL-----ESNRKVTKDR 405
Cdd:PRK04778  280 AEEKNEEIQERIDQLydilEREVKArkyVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTLneselESVRQLEKQL 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 406 TADGHALTEARKQLKEETQLRLDVEKELEvqigmrqEMELAMKMLEKDVCEKQDALVAL-------RQQLDDLRALKHEL 478
Cdd:PRK04778  358 ESLEKQYDEITERIAEQEIAYSELQEELE-------EILKQLEEIEKEQEKLSEMLQGLrkdeleaREKLERYRNKLHEI 430
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2077802608 479 SFKLQSSDM-GVKQksELNSRLEEKTNQMAATIKQLEQR 516
Cdd:PRK04778  431 KRYLEKSNLpGLPE--DYLEMFFEVSDEIEALAEELEEK 467
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
346-579 7.87e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 7.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 346 SATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQLKEETQL 425
Cdd:PRK02224  306 DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 426 RLDVEKELEvqigmrqEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSEL---------- 495
Cdd:PRK02224  386 IEELEEEIE-------ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALleagkcpecg 458
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 496 ------------------NSRLEEKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQ---------EFGDKINSLQLE 548
Cdd:PRK02224  459 qpvegsphvetieedrerVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERredleeliaERRETIEEKRER 538
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2077802608 549 VEELSRQRSHLELELKRERDRWSHSHQRSQE 579
Cdd:PRK02224  539 AEELRERAAELEAEAEEKREAAAEAEEEAEE 569
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
637-685 8.51e-04

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). 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. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.


Pssm-ID: 277275 [Multi-domain]  Cd Length: 56  Bit Score: 37.93  E-value: 8.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2077802608 637 ICQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELPLPSSI------NPERVCNPC 685
Cdd:cd15736     1 CCHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLNLSAydprngKWYRCCHSC 55
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
331-522 8.79e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  331 ILDQK--NYVEELnRHLSATVNNLQAKVDALEKSNTKLTEELAvaNNRIITLQEEMERVKEESSyileSNRKVTKDRTAD 408
Cdd:TIGR02169  748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVS----RIEARLREIEQK 820
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  409 GHALTEARKQLKEETQLRLDVEKELEVQIGM-RQEMELAMKMLEK---DVCEKQDALVALRQQLDDLRALKHELSFKLQS 484
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKEEleeELEELEAALRDLESRLGDLKKERDELEAQLRE 900
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2077802608  485 SDMGVKQKSELNSRLEEKTNQMAATIKQLEQRLQRAEK 522
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
292-589 8.85e-04

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 42.48  E-value: 8.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 292 NFCMKGEDLDSQVGVIDFSMYLKDGNSTKGSEGDGQITAILDQKNYVEELNRhlsaTVNNLQAKVDALEKSNTKLTEELa 371
Cdd:COG5391   232 RRVSTHPLLSNYKNSKSWESHSTLLSSFIENRKSVPTPLSLDLTSTTQELDM----ERKELNESTSKAIHNILSIFSLF- 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 372 vanNRIITLQEEME----RVKEESSYILESNRkvtkdrtaDGHALTEAR-KQLKEETQLRLDVEKELEVQIgmrqemeLA 446
Cdd:COG5391   307 ---EKILIQLESEEesltRLLESLNNLLLLVL--------NFSGVFAKRlEQNQNSILNEGVVQAETLRSS-------LK 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 447 MKMLEKDVCEKQ-DALVALRQQLDDLRALKHELSFKLQSSD-MGVKQKSELNSRLEEKT-----NQMAATIKQ----LEQ 515
Cdd:COG5391   369 ELLTQLQDEIKSrESLILTDSNLEKLTDQNLEDVEELSRSLrKNSSQRAVVSQQPEGLTsfsklSYKLRDFVQeksrSKS 448
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077802608 516 RLQRAEKDRQLAQQDNRLFK--QEFGDKINslqlevEELSRQRSHLELELKRERDRWSHSHQRSQENKKgtKNWLR 589
Cdd:COG5391   449 IESLQQDKEKLEEQLAIAEKdaQEINEELK------NELKFFFSVRNSDLEKILKSVADSHIEWAEENL--EIWKS 516
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
438-571 1.07e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  438 GMRQEMELA---MKMLEkDVCEKQDALVALRQQLDDLRALKHELSFKLQSsdmgvkQKSELnsrLEEKTNQMAATIKQLE 514
Cdd:COG4913    239 RAHEALEDAreqIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQ------RRLEL---LEAELEELRAELARLE 308
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2077802608  515 QRLQRAEKDRQLAQQDNRLFKQEfgdkINSLQLE-VEELSRQRSHLELELKRERDRWS 571
Cdd:COG4913    309 AELERLEARLDALREELDELEAQ----IRGNGGDrLEQLEREIERLERELEERERRRA 362
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
352-525 1.15e-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: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 352 LQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQLKEETQLR--LDV 429
Cdd:COG1579    15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEAL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 430 EKELEVQigmrqemELAMKMLEKDVCEKQDALVALRQQLDDLRAlkhelsfklqssdmgvkQKSELNSRLEEKTNQMAAT 509
Cdd:COG1579    95 QKEIESL-------KRRISDLEDEILELMERIEELEEELAELEA-----------------ELAELEAELEEKKAELDEE 150
                         170
                  ....*....|....*.
gi 2077802608 510 IKQLEQRLQRAEKDRQ 525
Cdd:COG1579   151 LAELEAELEELEAERE 166
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
221-589 1.28e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.03  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  221 VKDLPGLKTPVGRGRAWLRLA--LMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAI---IAGLLVGLNVIDANFCM 295
Cdd:pfam15921  316 MRQLSDLESTVSQLRSELREAkrMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLddqLQKLLADLHKREKELSL 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  296 KGE--------DLDSQVGVIDFSMYLKDGN----------STKGSEGDGQI---TAILDQKNyvEELNRhLSATVNNLQA 354
Cdd:pfam15921  396 EKEqnkrlwdrDTGNSITIDHLRRELDDRNmevqrleallKAMKSECQGQMerqMAAIQGKN--ESLEK-VSSLTAQLES 472
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  355 KVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQLKEETQLRlDVEKELE 434
Cdd:pfam15921  473 TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECE 551
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  435 VqigmrqemeLAMKMLEKDvcekqDALVALRQQLDDLRAL--------------KHELSFKLQSSDMGVKQKSELNSRLE 500
Cdd:pfam15921  552 A---------LKLQMAEKD-----KVIEILRQQIENMTQLvgqhgrtagamqveKAQLEKEINDRRLELQEFKILKDKKD 617
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  501 EKTNQMAATIKQLE-----------QRLqRAEKDrqLAQQDNRLFKQ--EFGDKINSLQLEVEELSRQRSHLELELKRER 567
Cdd:pfam15921  618 AKIRELEARVSDLElekvklvnagsERL-RAVKD--IKQERDQLLNEvkTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
                          410       420
                   ....*....|....*....|..
gi 2077802608  568 DRWSHSHQRSQENKKGTKNWLR 589
Cdd:pfam15921  695 NKLKMQLKSAQSELEQTRNTLK 716
PRK09039 PRK09039
peptidoglycan -binding protein;
410-557 1.72e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.10  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 410 HALTEARKQLKEETQLrLDVEKE----LEVQIGMRQEmELAMKMLEKDVCEKQDALVAlrQQLDDLRALKHELSFKL--- 482
Cdd:PRK09039   53 SALDRLNSQIAELADL-LSLERQgnqdLQDSVANLRA-SLSAAEAERSRLQALLAELA--GAGAAAEGRAGELAQELdse 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 483 -QSSDMGVKQKSELNSRLEEKTNQMAAtikqLEQRLQRAEKDRQlaQQDNRLfkQEFGDKINS-LQLEVEELSRQRS 557
Cdd:PRK09039  129 kQVSARALAQVELLNQQIAALRRQLAA----LEAALDASEKRDR--ESQAKI--ADLGRRLNVaLAQRVQELNRYRS 197
PRK11281 PRK11281
mechanosensitive channel MscK;
343-532 2.07e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.44  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  343 RHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKVTKDRTADGHALTEARKQLKEE 422
Cdd:PRK11281   117 TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAA----LYANSQRLQQIRNLLKGGKVGGKALRPS 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  423 TQLRLDVE-KELEVQIGMRQEmELAMKMLEKDVCEKQDALVALRQQL--DDLRALKHELSFK-LQSSDMGVKQKSELNSR 498
Cdd:PRK11281   193 QRVLLQAEqALLNAQNDLQRK-SLEGNTQLQDLLQKQRDYLTARIQRleHQLQLLQEAINSKrLTLSEKTVQEAQSQDEA 271
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2077802608  499 LEEKTN----QMAATIKQLEQRLQRA-EKDRQLAQQDNR 532
Cdd:PRK11281   272 ARIQANplvaQELEINLQLSQRLLKAtEKLNTLTQQNLR 310
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
338-649 2.25e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  338 VEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARK 417
Cdd:TIGR00606  693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  418 QLkEETQLRLDVEKELEVQIGMRQEMELAMKMLEKdvceKQDALVALRQQLDDLRALKhELSFKLQSSDM---GVKQKSE 494
Cdd:TIGR00606  773 LL-GTIMPEEESAKVCLTDVTIMERFQMELKDVER----KIAQQAAKLQGSDLDRTVQ-QVNQEKQEKQHeldTVVSKIE 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  495 LNSRLEEKTNQMAATIKQLEQRLqraeKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKRERDRWSHSH 574
Cdd:TIGR00606  847 LNRKLIQDQQEQIQHLKSKTNEL----KSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608  575 QRSQE--NKKGTKNWLRQDGKLRIQEENTNVKQPPREensvLPHKVPSGTQEEQEQLSGPGNTKICQLCQEEGSRTK 649
Cdd:TIGR00606  923 QEKEEliSSKETSNKKAQDKVNDIKEKVKNIHGYMKD----IENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEK 995
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
355-564 2.45e-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: 41.16  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 355 KVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyILESNRKVTKDrtadghaLTEARKQLKEETQLRLDVeKELE 434
Cdd:TIGR04523  97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ---KKENKKNIDKF-------LTEIKKKEKELEKLNNKY-NDLK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 435 VQIgmrQEMELAMKMLEKDVCEKQDALVALRQQlddLRALKHELSfKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLE 514
Cdd:TIGR04523 166 KQK---EELENELNLLEKEKLNIQKNIDKIKNK---LLKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ 238
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2077802608 515 QRLQRAEKDRQLAQQDNRLFKQEFGDKINSL---QLEVEELSRQRSHLELELK 564
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEQNNKKIKELEKQLN 291
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
424-591 2.49e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.14  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 424 QLRLDVEKELEvqigMRQEM-ELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDmgvKQKSELNSRLEEK 502
Cdd:pfam05262 185 ALREDNEKGVN----FRRDMtDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNAD---KQRDEVRQKQQEA 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 503 TN-------QMAATIKQL-EQRLQRAEKDRQLAQQDNRLFKQEFGDKINSLQLEVEELSRQRSHLELELKRERDRWSHSH 574
Cdd:pfam05262 258 KNlpkpadtSSPKEDKQVaENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDL 337
                         170
                  ....*....|....*..
gi 2077802608 575 QRSQENKKGTKNWLRQD 591
Cdd:pfam05262 338 QKTKPQVEAQPTSLNED 354
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
381-611 3.02e-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: 40.88  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 381 QEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQLKEETQLRLDVEKELE--VQIGMRQEME------LAMKM--- 449
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELEriRQEERKRELErirqeeIAMEIsrm 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 450 --LEKDVCEKQDALVALRQQLDDLRalkhelSFKLQSSDMGVKQKSELNSRLEEKTNQMAATikqlEQRLQRAEKDRQLA 527
Cdd:pfam17380 378 reLERLQMERQQKNERVRQELEAAR------KVKILEEERQRKIQQQKVEMEQIRAEQEEAR----QREVRRLEEERARE 447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 528 QQDNRLFKQEFGDKINSLQLEVEElsRQRSHLELElKRERDRwshshqrsqenkkgtknwlrqdgkLRIQEENTNVKQPP 607
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEEE--RKRKKLELE-KEKRDR------------------------KRAEEQRRKILEKE 500

                  ....
gi 2077802608 608 REEN 611
Cdd:pfam17380 501 LEER 504
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
335-569 3.21e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  335 KNYVEELNRHLSATVNnLQAKVDALEksntklteELAVANNRIITLQEEMERVKEESSYiLESNRKVTKDRTADgHALTE 414
Cdd:COG4913    231 VEHFDDLERAHEALED-AREQIELLE--------PIRELAERYAAARERLAELEYLRAA-LRLWFAQRRLELLE-AELEE 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  415 ARKQLKEETQLRLDVEKELEVQIGMRQEMELAM--------KMLEKDVCEKQDALVALRQQLDDLRALKHELSFKL-QSS 485
Cdd:COG4913    300 LRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLpASA 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  486 DMGVKQKSELNSRLEEKTNQMAAtikqLEQRLQRAEKDRQLAQQDnrlfkqefgdkINSLQLEVEELSRQRSHLELELKR 565
Cdd:COG4913    380 EEFAALRAEAAALLEALEEELEA----LEEALAEAEAALRDLRRE-----------LRELEAEIASLERRKSNIPARLLA 444

                   ....
gi 2077802608  566 ERDR 569
Cdd:COG4913    445 LRDA 448
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
348-565 3.37e-03

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.13  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 348 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKvtkdrtadghALTEARKQLKEETQLRL 427
Cdd:pfam09787  41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSRE----------QLQELEEQLATERSARR 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 428 DVEKELEvqigmRQEMELAmKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSdmgvKQKSELNSRLEEKTnqma 507
Cdd:pfam09787 111 EAEAELE-----RLQEELR-YLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSS----SSQSELENRLHQLT---- 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2077802608 508 atikqlEQRLQRaekdrqlaqqdnrlfkqefgdkinslQLEVEELSRQRSHLELELKR 565
Cdd:pfam09787 177 ------ETLIQK--------------------------QTMLEALSTEKNSLVLQLER 202
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
450-600 3.62e-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: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  450 LEKDVCEKQDALVALRQQLDDLRALKHELSfklqssdmgvkQKSELNSRLEE------KTNQMAATIKQLEQRLQRAEKD 523
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQ-----------ERREALQRLAEyswdeiDVASAEREIAELEAELERLDAS 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  524 ----RQLAQQdnrlfkqefgdkINSLQLEVEELSRQRSH-------LELELKRERDRWSHSHQRSQENKKGTKNWLRQDG 592
Cdd:COG4913    684 sddlAALEEQ------------LEELEAELEELEEELDElkgeigrLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751

                   ....*...
gi 2077802608  593 KLRIQEEN 600
Cdd:COG4913    752 EERFAAAL 759
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
638-686 4.64e-03

FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. 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 (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.


Pssm-ID: 277289 [Multi-domain]  Cd Length: 47  Bit Score: 35.41  E-value: 4.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2077802608 638 CQLCQEEGSRTKKKNVCKNCGGIFCEACSRNELplpssiNPERVCNPCH 686
Cdd:cd15750     3 CESCGAKFSVFKRKRTCADCKRYFCSNCLSKEE------RGRRRCRRCR 45
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
637-686 4.84e-03

FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.


Pssm-ID: 277263 [Multi-domain]  Cd Length: 61  Bit Score: 35.95  E-value: 4.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2077802608 637 ICQLCQEEG-SRTKKKNVCKNCGGIFCEACSRNELPLPS-SINPERVCNPCH 686
Cdd:cd15724     9 VCMVCQVERfSMFNRRHHCRRCGRVVCSSCSTKKMLVEGyRENPVRVCDQCY 60
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
648-689 6.42e-03

FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks 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. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.


Pssm-ID: 277262 [Multi-domain]  Cd Length: 62  Bit Score: 35.55  E-value: 6.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2077802608 648 TKKKNVCKNCGGIFCEACSRNELP--LPSSINPE------RVCNPCHKRL 689
Cdd:cd15723    13 LKKRRSCNNCGNAFCSRCCSKKVPrsVMGATAPAaqretvFVCSGCNDKL 62
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
353-576 7.23e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  353 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILE-------SNRKVTKDRTADGHALTEARKQLKEETQL 425
Cdd:TIGR00618  679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMHQARTVLKA 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  426 RLDVEKELEVQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRA-----LKHELSFKLQSSDMGVKQKSELNSRLE 500
Cdd:TIGR00618  759 RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAeigqeIPSDEDILNLQCETLVQEEEQFLSRLE 838
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077802608  501 EKTNQMAATIKQLEQRLQRAEKDRQLAQQDNRLFKQE---FGdkINSLQLEVEELSRQRSHLELELKRERDRWSHSHQR 576
Cdd:TIGR00618  839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSdklNG--INQIKIQFDGDALIKFLHEITLYANVRLANQSEGR 915
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
359-568 7.75e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.34  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 359 LEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGHALTEARKQLKEETQLRLDVEK------- 431
Cdd:pfam05557  32 LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREvisclkn 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608 432 ---ELEVQIgMRQEMELAMKMLEKDVcekqdalvaLRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEE------K 502
Cdd:pfam05557 112 elsELRRQI-QRAELELQSTNSELEE---------LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElefeiqS 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077802608 503 TNQMAATIKQLEQRLQR-AEKDRQLAQQdnrlfkQEFGDKINSLQLEVEELSRQRSHLELELKRERD 568
Cdd:pfam05557 182 QEQDSEIVKNSKSELARiPELEKELERL------REHNKHLNENIENKLLLKEEVEDLKRKLEREEK 242
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
335-553 8.67e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 8.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  335 KNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAvannriiTLQEEMERVKEESSYILESNRKVTKDRTADGHALTE 414
Cdd:pfam01576  400 KQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLS-------KLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077802608  415 ARKQLKEETQLRLDVEKELevqigmrqemelamKMLEkdvcekqDALVALRQQLDDLRALKHELSFKLQSSDMgvkQKSE 494
Cdd:pfam01576  473 TQELLQEETRQKLNLSTRL--------------RQLE-------DERNSLQEQLEEEEEAKRNVERQLSTLQA---QLSD 528
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077802608  495 LNSRLEEktnqMAATIKQLEQRLQRAEKDRQLAQQDNRLfKQEFGDKI----NSLQLEVEELS 553
Cdd:pfam01576  529 MKKKLEE----DAGTLEALEEGKKRLQRELEALTQQLEE-KAAAYDKLektkNRLQQELDDLL 586
 
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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