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Conserved domains on  [gi|568935999|ref|XP_006535179|]
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protein RUFY3 isoform X5 [Mus musculus]

Protein Classification

RUN and FYVE_RUFY3 domain-containing protein (domain architecture ID 13681779)

protein containing domains RUN, GBP_C, and FYVE_RUFY3

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
39-160 6.76e-43

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: 397055  Cd Length: 129  Bit Score: 149.34  E-value: 6.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   39 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 112
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568935999  113 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 160
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
497-543 7.12e-19

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: 80.15  E-value: 7.12e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568935999 497 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 543
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
208-438 1.74e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.42  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  208 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 285
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  286 KEETQLRLDVEKELELQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 364
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  365 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTRQRTQLELELKQ 431
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                  ....*..
gi 568935999  432 EKERKSQ 438
Cdd:COG1196   472 LQEELQR 478
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
39-160 6.76e-43

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: 397055  Cd Length: 129  Bit Score: 149.34  E-value: 6.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   39 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 112
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568935999  113 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 160
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
497-543 7.12e-19

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: 80.15  E-value: 7.12e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568935999 497 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 543
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
99-161 2.65e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 76.11  E-value: 2.65e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935999    99 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 161
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
491-546 1.33e-09

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: 54.36  E-value: 1.33e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   491 SEKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCHEQL 546
Cdd:smart00064   7 DEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
496-546 9.19e-09

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: 396091 [Multi-domain]  Cd Length: 68  Bit Score: 52.00  E-value: 9.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568935999  496 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCHEQL 546
Cdd:pfam01363  11 VCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTL 66
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
208-438 1.74e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.42  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  208 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 285
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  286 KEETQLRLDVEKELELQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 364
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  365 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTRQRTQLELELKQ 431
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                  ....*..
gi 568935999  432 EKERKSQ 438
Cdd:COG1196   472 LQEELQR 478
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
179-440 2.30e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   179 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 255
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   256 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 335
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   336 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 415
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*
gi 568935999   416 EALTRQRTQLELELKQEKERKSQNR 440
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELR 914
PRK11281 PRK11281
mechanosensitive channel MscK;
203-425 1.69e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  203 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEESSY----------LLESNRKGPKQDR- 271
Cdd:PRK11281  123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  272 ------TAEgQALSEA-----RKHLKEETQL------RLDvekELELQISmRQEMELA----------MKMLEKDVCEKQ 324
Cdd:PRK11281  192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRD---YLTARIQ-RLEHQLQllqeainskrLTLSEKTVQEAQ 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  325 DALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRleektNQMAATIKQLEQRLRQAERG--------RQSAELD 396
Cdd:PRK11281  267 SQDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTL-----TQQNLRVKNWLDRLTQSERNikeqisvlKGSLLLS 339
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568935999  397 NRLFKQ-----------DFGDKINSLQLEVEALTRQRTQL 425
Cdd:PRK11281  340 RILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
199-495 1.93e-04

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 44.13  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 199 QKNYVEELnRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRiitLQEEMERVKEESSYLLESNRKGPKQDRTAEgqal 278
Cdd:NF033930 103 QKAYVKYR-KAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAE---FNKVRAKVVPEAEELAETKKKAEEAKAEEP---- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 279 sEARKHLKEETQLRLDVEKELElqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG--VK 356
Cdd:NF033930 175 -VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSEdyIK 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 357 Q--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEK 433
Cdd:NF033930 243 EglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSDNNVA 322
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568935999 434 ERKSQnrgtpgkGAQKPelRMDGKHRIQEENVKLKKPLEEshrlLTHPAEEQGQPSLSEKPQ 495
Cdd:NF033930 323 DYYKE-------ALEKD--LATKKAELEKTQKDLDKALNE----LGPDGDEEETPAPAPQPE 371
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
220-387 2.17e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  220 KVDLLEKSNTKLTEELAVANNRIITLQE----------------EMERVKEES---SYLLESNRKGPKQDRTAEGQALSE 280
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  281 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQK 358
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKA 561
                         170       180       190
                  ....*....|....*....|....*....|.
gi 568935999  359 SELNSRLE--EKTNQMAATIKQLEQRLRQAE 387
Cdd:pfam17380 562 TEERSRLEamEREREMMRQIVESEKARAEYE 592
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
39-160 6.76e-43

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: 397055  Cd Length: 129  Bit Score: 149.34  E-value: 6.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   39 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 112
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568935999  113 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 160
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
497-543 7.12e-19

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: 80.15  E-value: 7.12e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568935999 497 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 543
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
99-161 2.65e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 76.11  E-value: 2.65e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935999    99 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 161
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
497-543 3.32e-17

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: 75.50  E-value: 3.32e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568935999 497 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCH 543
Cdd:cd15721   10 CQQCEKEFSLSrrKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
497-553 9.43e-15

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: 68.90  E-value: 9.43e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568935999 497 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIKQYSSS 553
Cdd:cd15759   13 CKLCEKEFSLSkrKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
497-551 6.52e-14

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: 66.63  E-value: 6.52e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568935999 497 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIKQYS 551
Cdd:cd15758   15 CKQCEKEFSISrrKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
497-543 9.50e-10

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


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 54.08  E-value: 9.50e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568935999 497 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCH 543
Cdd:cd00065    2 CMLCGKKFSLFrrRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
491-546 1.33e-09

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: 54.36  E-value: 1.33e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   491 SEKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCHEQL 546
Cdd:smart00064   7 DEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
496-543 3.13e-09

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: 52.92  E-value: 3.13e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568935999 496 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLP--SSIKPERVCNPCH 543
Cdd:cd15735    8 VCMRCRTAFTFTnrKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
497-542 5.30e-09

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: 52.40  E-value: 5.30e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568935999 497 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPC 542
Cdd:cd15730   12 CMACGKGFSVTvrKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDAC 59
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
496-546 9.19e-09

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: 396091 [Multi-domain]  Cd Length: 68  Bit Score: 52.00  E-value: 9.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568935999  496 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCHEQL 546
Cdd:pfam01363  11 VCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTL 66
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
496-546 1.71e-08

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: 50.85  E-value: 1.71e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568935999 496 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS-SI-KPERVCNPCHEQL 546
Cdd:cd15720    7 ECHRCRVQFGVFqrKHHCRACGQVFCGKCSSKSSTIPKfGIeKEVRVCDPCYEKL 61
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
208-438 1.74e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.42  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  208 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 285
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  286 KEETQLRLDVEKELELQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 364
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  365 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTRQRTQLELELKQ 431
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                  ....*..
gi 568935999  432 EKERKSQ 438
Cdd:COG1196   472 LQEELQR 478
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
497-542 3.49e-08

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: 50.02  E-value: 3.49e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568935999 497 CQLCQEDDS--LTKNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPC 542
Cdd:cd15734   11 CSVCKRPFSprLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
192-432 3.86e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 56.26  E-value: 3.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  192 QITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYL------LESNRK 265
Cdd:COG1196   689 ELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEELE 768
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  266 GPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 345
Cdd:COG1196   769 SLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELE 848
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  346 FKLQSSDlgvKQKSELNSRLEEKTNQMA----------ATIKQLEQRLRQAERGRQSAELDNrlfkQDFGDKINSLQLEV 415
Cdd:COG1196   849 EELEELE---KELEELKEELEELEAEKEeledelkeleEEKEELEEELRELESELAELKEEI----EKLRERLEELEAKL 921
                         250
                  ....*....|....*..
gi 568935999  416 EALTRQRTQLELELKQE 432
Cdd:COG1196   922 ERLEVELPELEEELEEE 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
179-440 2.30e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   179 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 255
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   256 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 335
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   336 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 415
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*
gi 568935999   416 EALTRQRTQLELELKQEKERKSQNR 440
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELR 914
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
505-542 2.35e-07

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


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 47.59  E-value: 2.35e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568935999 505 SLTKNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPC 542
Cdd:cd15732   21 ASRKHHCRNCGNVFCGSCCNQKLPVPSQqlFEPSRVCKSC 60
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
497-546 2.67e-07

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: 47.77  E-value: 2.67e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568935999 497 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCHEQL 546
Cdd:cd15719   12 CTGCSVRFSLTerRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
187-447 3.03e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 53.56  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  187 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESnrkg 266
Cdd:COG1196   719 EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE---- 794
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  267 pkqdRTAEGQALSEARKHLKEetqlrldVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 346
Cdd:COG1196   795 ----LEELEEELEEAERRLDA-------LERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKE 863
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  347 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQD---FGDKINSLQLEVEALTRQRT 423
Cdd:COG1196   864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKlerLEVELPELEEELEEEYEDTL 943
                         250       260
                  ....*....|....*....|....*
gi 568935999  424 QLELELKQEK-ERKSQNRGTPGKGA 447
Cdd:COG1196   944 ETELEREIERlEEEIEALGPVNLRA 968
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
204-487 4.61e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.79  E-value: 4.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  204 EELNRHLNATVNNL---QTKVDLLEKSNTKLTEELAVANnRIITLQEEMERvKEESSYLLESNRKGPKQDRTAEgqALSE 280
Cdd:COG1196   175 EEAERKLERTEENLerlEDLLEELEKQLEKLERQAEKAE-RYQELKAELRE-LELALLLAKLKELRKELEELEE--ELSR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  281 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-- 358
Cdd:COG1196   251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELke 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  359 --SELNSRLEEKTNQM---AATIKQLEQRLRQAE--RGRQSAELDNRlfKQDFGDKINSLQLEVEALTRQRTQLELE--- 428
Cdd:COG1196   331 kiEALKEELEERETLLeelEQLLAELEEAKEELEekLSALLEELEEL--FEALREELAELEAELAEIRNELEELKREies 408
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568935999  429 LKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEENVKLKKPLEESHRLLTHPAEEQGQ 487
Cdd:COG1196   409 LEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELER 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
200-441 6.27e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 6.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   200 KNYVEELNRhLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGpKQDRTAEGQALS 279
Cdd:TIGR02168  263 QELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   280 EARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSD------- 352
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrerlq 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   353 ---------LGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFkQDFGDKINSLQLEVEALTRQRT 423
Cdd:TIGR02168  421 qeieellkkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQE 499
                          250       260
                   ....*....|....*....|....
gi 568935999   424 QLE------LELKQEKERKSQNRG 441
Cdd:TIGR02168  500 NLEgfsegvKALLKNQSGLSGILG 523
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
492-542 7.76e-07

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: 46.22  E-value: 7.76e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568935999 492 EKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLP--SSIKPERVCNPC 542
Cdd:cd15727    8 KECPVCMSCKKKFDFFkrRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
508-542 9.72e-07

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


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 46.18  E-value: 9.72e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568935999 508 KNTCRNCRGTFCNACTTNELPLPSSI--KPERVCNPC 542
Cdd:cd15731   27 RHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
495-543 2.52e-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: 44.66  E-value: 2.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568935999 495 QVCQLCQEddslTKNT-------CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCH 543
Cdd:cd15717    9 PVCMHCKK----TKFTainrrhhCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
187-437 2.96e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 2.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   187 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssyllesnRKG 266
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   267 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 346
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   347 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRqaERGRQSAELDNRLfKQDFGDKINSLQLEVEALTRQRTQL- 425
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-ENKIEDDEEEARRRLKRLENKIKELg 985
                          250
                   ....*....|....*...
gi 568935999   426 ------ELELKQEKERKS 437
Cdd:TIGR02168  986 pvnlaaIEEYEELKERYD 1003
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
496-543 5.36e-06

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: 43.82  E-value: 5.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568935999 496 VCQLCQEDDSLTK--NTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCH 543
Cdd:cd15760    7 RCDVCRKKFGLFKrrHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
508-543 5.80e-06

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: 43.96  E-value: 5.80e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568935999 508 KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCH 543
Cdd:cd15733   23 KHHCRNCGNVFCADCSNYKLPIPDEqlYDPVRVCNSCY 60
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
210-453 8.21e-06

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 48.48  E-value: 8.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 210 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA---------LSE 280
Cdd:COG4372   79 IRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAqdlqtrlktLAE 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 281 ARKHLKEETQLRLDVEKELELQISM----RQEMELAMKMLE---KDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 353
Cdd:COG4372  159 QRRQLEAQAQSLQASQKQLQASATQlksqVLDLKLRSAQIEqeaQNLATRANAAQARTEELARRAAAAQQTAQAIQQRDA 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 354 GVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRT-------QLE 426
Cdd:COG4372  239 QISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQAAATQRGQVLAGAAQRVaqaqaqaQAQ 318
                        250       260       270
                 ....*....|....*....|....*....|
gi 568935999 427 LELKQEKERKS--QNRGTPGKG-AQKPELR 453
Cdd:COG4372  319 AQLLSSANRPAalRLRRSPRRGrRQRPVTR 348
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
245-465 1.80e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   245 LQEEMERVKEESsYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQ 324
Cdd:TIGR02169  672 EPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   325 DALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ 385
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   386 AERGRQSAELDNRLFK---QDFGDKINSLQLEVEALTRQRTQLELELKQEKERKsqnrgtpgKGAQKPELRMDGKHRIQE 462
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--------GDLKKERDELEAQLRELE 902

                   ...
gi 568935999   463 ENV 465
Cdd:TIGR02169  903 RKI 905
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
497-543 2.48e-05

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


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 41.72  E-value: 2.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568935999 497 CQLCQEDDSLTKNT--CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCH 543
Cdd:cd15749    2 CFGCAAKFSLFKKEcgCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
508-548 3.15e-05

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: 41.94  E-value: 3.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568935999 508 KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIK 548
Cdd:cd15739   26 KHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
199-388 4.38e-05

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 46.17  E-value: 4.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 199 QKNYV--EELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQ 276
Cdd:COG4372  129 RQNLAkaQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATR 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 277 AlsEARKHLKEETQLRLDVEKELELQISMR----QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS- 351
Cdd:COG4372  209 A--NAAQARTEELARRAAAAQQTAQAIQQRdaqiSQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYv 286
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568935999 352 DLGVKQKSELNSRLE----EKTNQMAATIKQLEQRLRQAER 388
Cdd:COG4372  287 RLRQQAAATQRGQVLagaaQRVAQAQAQAQAQAQLLSSANR 327
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
187-457 6.77e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 6.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   187 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEElavannRIITLQEEMERVKEESSYLLESNRKG 266
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   267 PKQDRTAEGQA----------LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQ 333
Cdd:TIGR02169  314 ERELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREK 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   334 LDDLralKHELAFKLQSSDLGVKQKSELNSRL----------EEKTNQMAATIKQLEQRLRQAERGRQSAELDnrlfKQD 403
Cdd:TIGR02169  394 LEKL---KREINELKRELDRLQEELQRLSEELadlnaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSK 466
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568935999   404 FGDKINSLQLEVEALTRQRTQLELELKQ-EKERKSQNRGTPGKGAQKPELRMDGK 457
Cdd:TIGR02169  467 YEQELYDLKEEYDRVEKELSKLQRELAEaEAQARASEERVRGGRAVEEVLKASIQ 521
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
496-546 8.16e-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: 40.79  E-value: 8.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568935999 496 VCQLCQEDDSLTKNT---CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCHEQL 546
Cdd:cd15755   10 VCMRCQKAKFTPVNRrhhCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
210-434 1.12e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.09  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  210 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAEGQALSEARKHLKEET 289
Cdd:COG1196   300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLE-ELEQLLAELEEAKEELEEKLSALLEELEELF 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  290 QLRLDVEKELELQISMRQEmelAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKT 369
Cdd:COG1196   379 EALREELAELEAELAEIRN---ELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQL 455
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935999  370 NQMAATIKQLEQRLRQAERGRQSAELDnrlfKQDFGDKINSLQLEVEALTRQRTQLELELKQEKE 434
Cdd:COG1196   456 EELRDRLKELERELAELQEELQRLEKE----LSSLEARLDRLEAEQRASQGVRAVLEALESGLPG 516
PRK11281 PRK11281
mechanosensitive channel MscK;
203-425 1.69e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  203 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEESSY----------LLESNRKGPKQDR- 271
Cdd:PRK11281  123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  272 ------TAEgQALSEA-----RKHLKEETQL------RLDvekELELQISmRQEMELA----------MKMLEKDVCEKQ 324
Cdd:PRK11281  192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRD---YLTARIQ-RLEHQLQllqeainskrLTLSEKTVQEAQ 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  325 DALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRleektNQMAATIKQLEQRLRQAERG--------RQSAELD 396
Cdd:PRK11281  267 SQDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTL-----TQQNLRVKNWLDRLTQSERNikeqisvlKGSLLLS 339
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568935999  397 NRLFKQ-----------DFGDKINSLQLEVEALTRQRTQL 425
Cdd:PRK11281  340 RILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
199-495 1.93e-04

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 44.13  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 199 QKNYVEELnRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRiitLQEEMERVKEESSYLLESNRKGPKQDRTAEgqal 278
Cdd:NF033930 103 QKAYVKYR-KAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAE---FNKVRAKVVPEAEELAETKKKAEEAKAEEP---- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 279 sEARKHLKEETQLRLDVEKELElqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG--VK 356
Cdd:NF033930 175 -VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSEdyIK 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 357 Q--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEK 433
Cdd:NF033930 243 EglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSDNNVA 322
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568935999 434 ERKSQnrgtpgkGAQKPelRMDGKHRIQEENVKLKKPLEEshrlLTHPAEEQGQPSLSEKPQ 495
Cdd:NF033930 323 DYYKE-------ALEKD--LATKKAELEKTQKDLDKALNE----LGPDGDEEETPAPAPQPE 371
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
204-479 2.01e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 44.37  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 204 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARK 283
Cdd:COG0419  170 EKLSELLKEVIKEAKAKIEELEG---QLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEE 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 284 HLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQdalvslrQQLDDLRALKHELAFKLQSSDLGVKQKSELNS 363
Cdd:COG0419  247 EKERLEELKARLLEIESLELEALKIREEELRELERLLEELE-------EKIERLEELEREIEELEEELEGLRALLEELEE 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 364 RLEEktnqmaatIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGTP 443
Cdd:COG0419  320 LLEK--------LKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAI 391
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568935999 444 GKGAQKPELRMDGKHRIQEENVKLKKPLEESHRLLT 479
Cdd:COG0419  392 QELKEELAELSAALEEIQEELEELEKELEELERELE 427
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
220-387 2.17e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  220 KVDLLEKSNTKLTEELAVANNRIITLQE----------------EMERVKEES---SYLLESNRKGPKQDRTAEGQALSE 280
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  281 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQK 358
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKA 561
                         170       180       190
                  ....*....|....*....|....*....|.
gi 568935999  359 SELNSRLE--EKTNQMAATIKQLEQRLRQAE 387
Cdd:pfam17380 562 TEERSRLEamEREREMMRQIVESEKARAEYE 592
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
204-434 2.82e-04

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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   204 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALS 279
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLEEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   280 EARKHLKEE-------TQLRL-------DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 345
Cdd:pfam01576  163 EFTSNLAEEeekvkslNKLKNkheamisDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAKKE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   346 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVE-ALTRQRTQ 424
Cdd:pfam01576  243 EELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRR----DLGEELEALKTELEdTLDSTAAQ 318
                          250
                   ....*....|
gi 568935999   425 LELELKQEKE 434
Cdd:pfam01576  319 QELRSKREQE 328
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
217-386 5.81e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.73  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  217 LQTKVDLLEKSNTKLTE-----ELAVANNRIITLQEEMERVKEESSYLLESNRKGPkqdrTAEGQALSEARKhlKEETQL 291
Cdd:PRK10929  112 LQVSSQLLEKSRQAQQEqdrarEISDSLSQLPQQQTEARRQLNEIERRLQTLGTPN----TPLAQAQLTALQ--AESAAL 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  292 RLDVEkELEL-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL------QSSDL--GVKQKS 359
Cdd:PRK10929  186 KALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEStellaeQSGDLpkSIVAQF 264
                         170       180
                  ....*....|....*....|....*..
gi 568935999  360 ELNSRLEEKTNQMAATIKQLEQRLRQA 386
Cdd:PRK10929  265 KINRELSQALNQQAQRMDLIASQQRQA 291
mukB PRK04863
chromosome partition protein MukB;
278-440 5.99e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 5.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  278 LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 355
Cdd:PRK04863  444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  356 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAErGRQSAELDNRLFKQDF----GDKINSLQLEVEALTRQRTQLELELK 430
Cdd:PRK04863  519 RMRlSELEQRLRQQ--------QRAERLLAEFC-KRLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589
                         170
                  ....*....|
gi 568935999  431 QEKERKSQNR 440
Cdd:PRK04863  590 QLQARIQRLA 599
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
497-542 6.17e-04

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  Cd Length: 58  Bit Score: 37.92  E-value: 6.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568935999 497 CQLCQEDDS--LTKNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPC 542
Cdd:cd15726   10 CLDCKSEFSwmVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
204-440 6.40e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 42.44  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 204 EELNRHLNATVNNLQTKVDLLEKSNTKLtEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARK 283
Cdd:COG0419  318 EELLEKLKSLEERLEKLEEKLEKLESEL-EELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKE 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 284 HLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAL------------KHELAFKLQSS 351
Cdd:COG0419  397 ELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELagagekcpvcgqELPEEHEKELL 476
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 352 DLGVKQKSELNSRL--EEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELEL 429
Cdd:COG0419  477 ELYELELEELEEELsrEKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQ 556
                        250
                 ....*....|.
gi 568935999 430 KQEKERKSQNR 440
Cdd:COG0419  557 LKEELRQLEDR 567
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
194-367 1.09e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.01  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  194 TAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRkgpkqDRTA 273
Cdd:COG1196   351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLE-----DLKE 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  274 EGQALSEARKHLKEETQLRLDVEKELELQISMRQEmelAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 353
Cdd:COG1196   426 ELKELEAELEELQTELEELNEELEELEEQLEELRD---RLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
                         170
                  ....*....|....
gi 568935999  354 GVKQKSELNSRLEE 367
Cdd:COG1196   503 VRAVLEALESGLPG 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
192-344 1.34e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   192 QITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNT-------KLTEELAVANNRIITLQEEMERvkeessylLESNR 264
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLER--------LEDRR 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   265 KGPKQDRTAEGQALSEARkhlKEETQLRLD-VEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHE 343
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEAE---LKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493

                   .
gi 568935999   344 L 344
Cdd:TIGR02168  494 L 494
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
497-542 1.35e-03

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: 36.71  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568935999 497 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKP--ERVCNPC 542
Cdd:cd15745    2 CAICAKAFSLFrrKYVCRLCGGVVCHSCSSEDLVLSVPDTCiyLRVCKTC 51
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
491-546 1.36e-03

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


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 37.33  E-value: 1.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568935999 491 SEKPQvCQLCQEDDSLTK--NTCRNCRGTFCNACTTNELPLPS-SIKPERVCNPCHEQL 546
Cdd:cd15729   11 SEAPN-CMQCEVKFTFTKrrHHCRACGKVLCSACCSLKARLEYlDNKEARVCVPCYQTL 68
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
213-387 1.44e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 213 TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgqalSEARKHLKEETQLR 292
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 293 L-DVEKELELQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 371
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                        170
                 ....*....|....*.
gi 568935999 372 MAATIKQLEQRLRQAE 387
Cdd:PRK03918 537 LKGEIKSLKKELEKLE 552
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
508-543 1.63e-03

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  Cd Length: 61  Bit Score: 36.92  E-value: 1.63e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568935999 508 KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCH 543
Cdd:cd15738   24 KHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
205-382 1.82e-03

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 40.82  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 205 ELNRhLNATVNNLQTKVDLL--------------EKSNTKLTEELAVANNRIITLQEEMERVKEesSYLLESNRKGPKQD 270
Cdd:COG4477  275 ELDE-AEEELGLIQEKIESLydllereveaknvvEENLPILPDYLEKAKENNEHLKEEIERVKE--SYRLAETELGSVRK 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 271 RTAEGQALSEARKHLKEETQLRLDVEKELElqiSMRQEMELAMKMLEKDVCEKQDALVSLR-------QQLDDLRALKHE 343
Cdd:COG4477  352 FEKELKELESVLDEILENIEAQEVAYSELQ---DNLEEIEKALTDIEDEQEKVQEHLTSLRkdelearENLERLKSKLHE 428
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568935999 344 LAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 382
Cdd:COG4477  429 IKRYMEKSNLpGLPE--TFLSLFFTAGHEIQDLMKELSEV 466
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
263-473 2.06e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.85  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  263 NRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELElqismrqEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKH 342
Cdd:COG1196   647 EPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLE-------KLEEELKSLKNELRSLEDLLEELRRQLEELERQLE 719
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  343 ELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEALTRQR 422
Cdd:COG1196   720 ELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLE-----------EALAKLKEEIEELEEKR 788
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568935999  423 TQLELELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEENVKLKKPLEE 473
Cdd:COG1196   789 QALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEE 839
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
192-498 2.14e-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: 41.11  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   192 QITAILDQknyvEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMErvkeessyLLESNRKGPKQDR 271
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAE--------LCAAAITCTAQCE 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   272 TAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEME---LAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL 348
Cdd:TIGR00618  455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   349 QSSDLGVKQKSELNSRLEEKTNQmAATIKQLEQRLRQAE------RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQR 422
Cdd:TIGR00618  535 QTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFsiltqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568935999   423 TQLELELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEEnvkLKKPLEESHRLLTHPAEEQGQPSLSEKPQVCQ 498
Cdd:TIGR00618  614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT---LTQERVREHALSIRVLPKELLASRQLALQKMQ 686
YloA COG1293
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ...
306-469 2.78e-03

Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains fibronectin-binding (FbpA) and DUF814 domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 224212 [Multi-domain]  Cd Length: 564  Bit Score: 40.45  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 306 RQEMELAMKMLEKDVC---EKQDALVSLRQqLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQR 382
Cdd:COG1293  230 REALEELLNPLKPNYYykdEKYLDVVPLKA-YADLEKLFNEALDEKFERDKIKQLASELEKKLEKELKKLENKLEKQEDE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 383 LRQAERgrqsaeLDNRLFKQdfGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGTPGKGAQ---KPELRMDGKHR 459
Cdd:COG1293  309 LEELEK------AAEELRQK--GELLYANLQLIEEGLKSVRLADFYGNEEIKIELDKSKTPSENAQryfKKYKKLKGAKV 380
                        170
                 ....*....|
gi 568935999 460 IQEENVKLKK 469
Cdd:COG1293  381 NLDRQLSELK 390
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
196-483 3.20e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 40.64  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  196 ILDQKNYV-EELNRHLNATVNNLQTKVDLLEKSNTKlTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAE 274
Cdd:COG3096   263 ISEATNYVaADYMRHANERRVHLDQALEFRRELYTS-RQQLAAEQYRHVDMSRELAELNGAEG-DLEADYQAASDHLNLV 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  275 GQALSEARKHLK-----EETQLRLDVEKELELQISMRQ-EMELAMKMLEKDVCEKQDALVSLRQQLD--DLRALKHELAF 346
Cdd:COG3096   341 QTALRQQEKIERyqadlEELTIRLEEQNEVVEEANERQeENEARAEAAELEVDELKSQLADYQQALDvqQTRAIQYQQAI 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  347 K--------LQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGdkinslqlEVEAL 418
Cdd:COG3096   421 AalerakelCHLPDLTADSAEEWLETFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAG--------ELARS 492
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935999  419 TRQRTQLELeLKQEKERKSQNRGTPGKGAQKPELrmDGKHRIQEENVKLKKPLEESHRLLTHPAE 483
Cdd:COG3096   493 EAWDVAREL-LREGPDQRHLAEQVQPLRMRLSEL--EQRLRQQQSAERLLADFCKRQGKNLDAEE 554
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
183-428 3.61e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   183 SSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLES 262
Cdd:TIGR02169  708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   263 NRKGPKQDRTAEGQALSEARKHLKEETQlrlDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKH 342
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999   343 ELAFKLQSSDLGVKQ-------------------------KSELNSRLEEKT---NQMAATIKQLEQRLRQAErgrqsae 394
Cdd:TIGR02169  865 ELEEELEELEAALRDlesrlgdlkkerdeleaqlrelerkIEELEAQIEKKRkrlSELKAKLEALEEELSEIE------- 937
                          250       260       270
                   ....*....|....*....|....*....|....
gi 568935999   395 ldnRLFKQDFGDKINSLQLEVEALTRQRTQLELE 428
Cdd:TIGR02169  938 ---DPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
195-438 4.03e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 40.13  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 195 AILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLES-NRKGPKQDRTA 273
Cdd:COG0419  484 EELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKlQLQQLKEELRQ 563
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 274 EGQALSEARKHLKEETQLRLDVEKELELQISMRQ----EMELAMKMLEK----DVCEKQDALVSLRQQLDDLRALKHELA 345
Cdd:COG0419  564 LEDRLQELKELLEELRLLRTRKEELEELRERLKElkkkLKELEERLSQLeellQSLELSEAENELEEAEEELESELEKLN 643
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 346 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTR 420
Cdd:COG0419  644 LQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQlreelEELLKKLGEIEQLIEELES 723
                        250
                 ....*....|....*...
gi 568935999 421 QRTQLElELKQEKERKSQ 438
Cdd:COG0419  724 RKAELE-ELKKELEKLEK 740
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
246-493 6.46e-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: 39.34  E-value: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  246 QEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARKHLKEEtqlRLDVEKELELQiSMRQE-----------MELAMK 314
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE---RMAMERERELE-RIRQEerkrelerirqEEIAME 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  315 M-----LEKDVCEKQDALVSLRQQLDDLRALK---HELAFKLQssdlgvKQKSELNSRLEEKTNQMAATIKQLEQ-RLRQ 385
Cdd:pfam17380 374 IsrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQ------QQKVEMEQIRAEQEEARQREVRRLEEeRARE 447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999  386 AERGRQsaeldnrlfkqdfgdkinslqlevEALTRQRtQLELELKQEKERKSQnrgtpgKGAQKPELRmdGKHRIQEENV 465
Cdd:pfam17380 448 MERVRL------------------------EEQERQQ-QVERLRQQEEERKRK------KLELEKEKR--DRKRAEEQRR 494
                         250       260
                  ....*....|....*....|....*....
gi 568935999  466 K-LKKPLEESHRLLThpaEEQGQPSLSEK 493
Cdd:pfam17380 495 KiLEKELEERKQAMI---EEERKRKLLEK 520
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
196-438 7.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 196 ILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIitlqEEMERVKEESSYLLESNRKGPKQDRTAEg 275
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLE- 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 276 QALSEARKHLkEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGV 355
Cdd:PRK03918 259 EKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 356 KQKSELNSRLEEKTNQMAAtikqLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKER 435
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413

                 ...
gi 568935999 436 KSQ 438
Cdd:PRK03918 414 IGE 416
YhaN COG4717
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
229-448 7.72e-03

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


Pssm-ID: 227061 [Multi-domain]  Cd Length: 984  Bit Score: 39.06  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 229 TKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELelqismRQE 308
Cdd:COG4717  277 EKREAHLQKTEAEIDALLVRLAELKDLAS-QLIPAKEAVLQALVRLHQQLSEIKASAFELTETLAGIEADL------RDK 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935999 309 MELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAfklqssdlgvkqksELNSRLEEKTNQMAATIKQLEQRLRQAE- 387
Cdd:COG4717  350 EEAAGNGFEAERVHDLRSLECMLRYQSSQRELKQTEA--------------AYCKRLDEKRLFEDEAEEEARQRLADDEe 415
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568935999 388 --RGRQSAELDNRLFKQDFGDKINSLQLEVEALT---RQRTQLELELKQEKERKSQNRGTPGKGAQ 448
Cdd:COG4717  416 evRAGDEAREEKIAANSQVIDKEEVCNLYDRRDTawqKQRFLREKQTAFERQKTEHTKIIALRLAG 481
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
497-545 9.92e-03

FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which 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.


Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 34.66  E-value: 9.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568935999 497 CQLCQED------DSLTKNTCRNCRGTFCNACTTNELPLPSSIKpERVCNPCHEQ 545
Cdd:cd15776    3 CPLCKTElnigskDPPNFNTCTECKKTVCNLCGFNPTPHLTEVK-EWLCLNCQTQ 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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