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Conserved domains on  [gi|576795839|ref|NP_001276703|]
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protein RUFY3 isoform 1 [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 ...
153-274 3.44e-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: 151.65  E-value: 3.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  153 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 226
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 576795839  227 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 274
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
611-657 6.57e-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: 80.54  E-value: 6.57e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576795839 611 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 657
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
322-552 5.21e-10

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: 62.81  E-value: 5.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  322 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 399
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  400 KEETQLRLDVEKELELQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 478
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  479 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTRQRTQLELELKQ 545
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                  ....*..
gi 576795839  546 EKERKSQ 552
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 ...
153-274 3.44e-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: 151.65  E-value: 3.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  153 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 226
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 576795839  227 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 274
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
611-657 6.57e-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: 80.54  E-value: 6.57e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576795839 611 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 657
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
213-275 6.31e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 78.04  E-value: 6.31e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576795839   213 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 275
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
322-552 5.21e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 62.81  E-value: 5.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  322 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 399
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  400 KEETQLRLDVEKELELQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 478
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  479 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTRQRTQLELELKQ 545
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                  ....*..
gi 576795839  546 EKERKSQ 552
Cdd:COG1196   472 LQEELQR 478
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
605-660 1.61e-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: 1.61e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   605 SEKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCHEQL 660
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: ...
610-660 1.12e-08

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: 1.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839  610 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCHEQL 660
Cdd:pfam01363  11 VCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
293-554 3.17e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 3.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   293 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 369
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   370 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 449
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   450 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 529
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*
gi 576795839   530 EALTRQRTQLELELKQEKERKSQNR 554
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELR 914
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
318-548 1.23e-05

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


Pssm-ID: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 48.63  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   318 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALS 393
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLEEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   394 EARKHLKEE-------TQLRL-------DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 459
Cdd:pfam01576  163 EFTSNLAEEeekvkslNKLKNkheamisDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAKKE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   460 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVE-ALTRQRTQ 538
Cdd:pfam01576  243 EELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRR----DLGEELEALKTELEdTLDSTAAQ 318
                          250
                   ....*....|
gi 576795839   539 LELELKQEKE 548
Cdd:pfam01576  319 QELRSKREQE 328
PRK11281 PRK11281
mechanosensitive channel MscK;
317-539 2.15e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.98  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  317 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEESSY----------LLESNRKGPKQDR- 385
Cdd:PRK11281  123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  386 ------TAEgQALSEA-----RKHLKEETQL------RLDvekELELQISmRQEMELA----------MKMLEKDVCEKQ 438
Cdd:PRK11281  192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRD---YLTARIQ-RLEHQLQllqeainskrLTLSEKTVQEAQ 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  439 DALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERG--------RQSAELD 510
Cdd:PRK11281  267 SQDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLS 339
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 576795839  511 NRLFKQ-----------DFGDKINSLQLEVEALTRQRTQL 539
Cdd:PRK11281  340 RILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
313-609 3.27e-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: 43.75  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 313 QKNYVEELnRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRiitLQEEMERVKEESSYLLESNRKGPKQDRTAEgqal 392
Cdd:NF033930 103 QKAYVKYR-KAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAE---FNKVRAKVVPEAEELAETKKKAEEAKAEEP---- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 393 sEARKHLKEETQLRLDVEKELElqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG--VK 470
Cdd:NF033930 175 -VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSEdyIK 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 471 Q--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEK 547
Cdd:NF033930 243 EglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSDNNVA 322
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576795839 548 ERKSQnrgtpgkGAQKPelRMDGKHRIQEENVKLKKPLEEshrlLTHPAEEQGQPSLSEKPQ 609
Cdd:NF033930 323 DYYKE-------ALEKD--LATKKAELEKTQKDLDKALNE----LGPDGDEEETPAPAPQPE 371
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
153-274 3.44e-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: 151.65  E-value: 3.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  153 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 226
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 576795839  227 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 274
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
611-657 6.57e-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: 80.54  E-value: 6.57e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576795839 611 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 657
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
213-275 6.31e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 78.04  E-value: 6.31e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576795839   213 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 275
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
611-657 3.34e-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: 75.88  E-value: 3.34e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCH 657
Cdd:cd15721   10 CQQCEKEFSLSrrKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
611-667 1.03e-14

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


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 69.28  E-value: 1.03e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIKQYSSS 667
Cdd:cd15759   13 CKLCEKEFSLSkrKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
611-665 5.30e-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: 67.01  E-value: 5.30e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIKQYS 665
Cdd:cd15758   15 CKQCEKEFSISrrKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
322-552 5.21e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 62.81  E-value: 5.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  322 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 399
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  400 KEETQLRLDVEKELELQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 478
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  479 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTRQRTQLELELKQ 545
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                  ....*..
gi 576795839  546 EKERKSQ 552
Cdd:COG1196   472 LQEELQR 478
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
611-657 8.14e-10

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


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 54.85  E-value: 8.14e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCH 657
Cdd:cd00065    2 CMLCGKKFSLFrrRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
308-546 1.27e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 61.65  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  308 TAILDQKNYVEELNRHLNA---TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYL------LESNR 378
Cdd:COG1196   688 EELKSLKNELRSLEDLLEElrrQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEEL 767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  379 KGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 458
Cdd:COG1196   768 ESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  459 AFKLQSSDlgvKQKSELNSRLEEKTNQMA----------ATIKQLEQRLRQAERGRQSAELDNrlfkQDFGDKINSLQLE 528
Cdd:COG1196   848 EEELEELE---KELEELKEELEELEAEKEeledelkeleEEKEELEEELRELESELAELKEEI----EKLRERLEELEAK 920
                         250
                  ....*....|....*...
gi 576795839  529 VEALTRQRTQLELELKQE 546
Cdd:COG1196   921 LERLEVELPELEEELEEE 938
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
605-660 1.61e-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: 1.61e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   605 SEKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCHEQL 660
Cdd:smart00064   7 DEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
610-657 3.79e-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: 3.79e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576795839 610 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLP--SSIKPERVCNPCH 657
Cdd:cd15735    8 VCMRCRTAFTFTnrKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
611-656 6.42e-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: 6.42e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPC 656
Cdd:cd15730   12 CMACGKGFSVTvrKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDAC 59
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
318-601 9.93e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.57  E-value: 9.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  318 EELNRHLNATVNNL---QTKVDLLEKSNTKLTEELAVANnRIITLQEEMERvKEESSYLLESNRKGPKQDRTAEgqALSE 394
Cdd:COG1196   175 EEAERKLERTEENLerlEDLLEELEKQLEKLERQAEKAE-RYQELKAELRE-LELALLLAKLKELRKELEELEE--ELSR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  395 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-- 472
Cdd:COG1196   251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELke 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  473 --SELNSRLEEKTNQM---AATIKQLEQRLRQAE--RGRQSAELDNRlfKQDFGDKINSLQLEVEALTRQRTQLELE--- 542
Cdd:COG1196   331 kiEALKEELEERETLLeelEQLLAELEEAKEELEekLSALLEELEEL--FEALREELAELEAELAEIRNELEELKREies 408
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 576795839  543 LKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEENVKLKKPLEESHRLLTHPAEEQGQ 601
Cdd:COG1196   409 LEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELER 467
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
610-660 1.12e-08

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: 1.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839  610 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCHEQL 660
Cdd:pfam01363  11 VCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTL 66
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
610-660 1.53e-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: 51.23  E-value: 1.53e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 610 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS-SI-KPERVCNPCHEQL 660
Cdd:cd15720    7 ECHRCRVQFGVFqrKHHCRACGQVFCGKCSSKSSTIPKfGIeKEVRVCDPCYEKL 61
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
301-561 1.56e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.19  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  301 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESnrkg 380
Cdd:COG1196   719 EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE---- 794
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  381 pkqdRTAEGQALSEARKHLKEetqlrldVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 460
Cdd:COG1196   795 ----LEELEEELEEAERRLDA-------LERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKE 863
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  461 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFK---QDFGDKINSLQLEVEALTRQRT 537
Cdd:COG1196   864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEaklERLEVELPELEEELEEEYEDTL 943
                         250       260
                  ....*....|....*....|....*
gi 576795839  538 QLELELKQEK-ERKSQNRGTPGKGA 561
Cdd:COG1196   944 ETELEREIERlEEEIEALGPVNLRA 968
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
293-554 3.17e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 3.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   293 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 369
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   370 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 449
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   450 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 529
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*
gi 576795839   530 EALTRQRTQLELELKQEKERKSQNR 554
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELR 914
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
611-656 4.23e-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: 4.23e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 576795839 611 CQLCQEDDS--LTKNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPC 656
Cdd:cd15734   11 CSVCKRPFSprLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-555 6.55e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 6.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   314 KNYVEELNRhLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGpKQDRTAEGQALS 393
Cdd:TIGR02168  263 QELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   394 EARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRA-----------LKHELAFKL 462
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierlearlerLEDRRERLQ 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   463 Q-----SSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFkQDFGDKINSLQLEVEALTRQRT 537
Cdd:TIGR02168  421 QeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQE 499
                          250       260
                   ....*....|....*....|....
gi 576795839   538 QLE------LELKQEKERKSQNRG 555
Cdd:TIGR02168  500 NLEgfsegvKALLKNQSGLSGILG 523
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
297-551 8.26e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 55.88  E-value: 8.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  297 SSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssylles 376
Cdd:COG1196   708 RRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEE------- 780
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  377 nrkgpkqdrtaegqaLSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKH 456
Cdd:COG1196   781 ---------------IEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLD 845
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  457 ELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEALTRQR 536
Cdd:COG1196   846 ELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELE-----------SELAELKEEIEKLRERL 914
                         250
                  ....*....|....*
gi 576795839  537 TQLELELKQEKERKS 551
Cdd:COG1196   915 EELEAKLERLEVELP 929
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
611-660 1.49e-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: 48.54  E-value: 1.49e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCHEQL 660
Cdd:cd15719   12 CTGCSVRFSLTerRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
619-656 2.85e-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: 2.85e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 576795839 619 SLTKNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPC 656
Cdd:cd15732   21 ASRKHHCRNCGNVFCGSCCNQKLPVPSQqlFEPSRVCKSC 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-551 4.66e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   301 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssyllesnRKG 380
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   381 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 460
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   461 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRqaERGRQSAELDNRLfKQDFGDKINSLQLEVEALTRQRTQL- 539
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-ENKIEDDEEEARRRLKRLENKIKELg 985
                          250
                   ....*....|....*...
gi 576795839   540 ------ELELKQEKERKS 551
Cdd:TIGR02168  986 pvnlaaIEEYEELKERYD 1003
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
606-656 9.41e-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: 9.41e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 606 EKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLP--SSIKPERVCNPC 656
Cdd:cd15727    8 KECPVCMSCKKKFDFFkrRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
622-656 1.18e-06

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: 1.18e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 576795839 622 KNTCRNCRGTFCNACTTNELPLPSSI--KPERVCNPC 656
Cdd:cd15731   27 RHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
359-579 2.67e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   359 LQEEMERVKEESsYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQ 438
Cdd:TIGR02169  672 EPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   439 DALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ 499
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   500 AERGRQSAELDNRLFK---QDFGDKINSLQLEVEALTRQRTQLELELKQEKERKsqnrgtpgKGAQKPELRMDGKHRIQE 576
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--------GDLKKERDELEAQLRELE 902

                   ...
gi 576795839   577 ENV 579
Cdd:TIGR02169  903 RKI 905
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
324-588 2.74e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  324 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEsSYLLESNRKGPK---QDRTAEGQALSEARKHLK 400
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE-IKNLESQINDLEskiQNQEKLNQQKDEQIKKLQ 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  401 EETQLrldVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSL-------RQQLDDL----RALKHELAFKLQSSDLGV 469
Cdd:TIGR04523 419 QEKEL---LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLsrsiNKIKQNLEQKQKELKSKE 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  470 KQKSELN---SRLEEKTNQMAATIKQLEQRLRQ-----AERGRQSAELDNRLFKQDFG--------------DKINSLQL 527
Cdd:TIGR04523 496 KELKKLNeekKELEEKVKDLTKKISSLKEKIEKlesekKEKESKISDLEDELNKDDFElkkenlekeideknKEIEELKQ 575
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795839  528 EVEALTRQRTQLELELKQ-EKERKSQNRGTPGKGAQKPELRMDGKHrIQEENVKL---KKPLEES 588
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQkEKEKKDLIKEIEEKEKKISSLEKELEK-AKKENEKLssiIKNIKSK 639
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
609-657 3.05e-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: 3.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 576795839 609 QVCQLCQEddslTKNT-------CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCH 657
Cdd:cd15717    9 PVCMHCKK----TKFTainrrhhCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
289-593 3.79e-06

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 50.14  E-value: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 289 SMYLKDGN-----SSKGSEGDGQITAILDQKNYvEELNRHLNATVNNLQTKVDLLEKsntKLTEELAVANNRIITLQEEM 363
Cdd:COG0419  137 SVYLPQGEfdaflKSKPKERKEILDELFGLEKY-EKLSELLKEVIKEAKAKIEELEG---QLSELLEDIEDLLEALEEEL 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 364 ERVKEESSYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQdalvs 443
Cdd:COG0419  213 KELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELE----- 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 444 lrQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEktnqmaatIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKIN 523
Cdd:COG0419  288 --EKIERLEELEREIEELEEELEGLRALLEELEELLEK--------LKSLEERLEKLEEKLEKLESELEELAEEKNELAK 357
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 524 SLQLEVEALTRQRTQLELELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEENVKLKKPLEESHRLLT 593
Cdd:COG0419  358 LLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELE 427
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
324-567 5.84e-06

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 49.25  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 324 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA---------LSE 394
Cdd:COG4372   79 IRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAqdlqtrlktLAE 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 395 ARKHLKEETQLRLDVEKELELQISM----RQEMELAMKMLE---KDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 467
Cdd:COG4372  159 QRRQLEAQAQSLQASQKQLQASATQlksqVLDLKLRSAQIEqeaQNLATRANAAQARTEELARRAAAAQQTAQAIQQRDA 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 468 GVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRT-------QLE 540
Cdd:COG4372  239 QISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQAAATQRGQVLAGAAQRVaqaqaqaQAQ 318
                        250       260       270
                 ....*....|....*....|....*....|
gi 576795839 541 LELKQEKERKS--QNRGTPGKG-AQKPELR 567
Cdd:COG4372  319 AQLLSSANRPAalRLRRSPRRGrRQRPVTR 348
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
610-657 6.48e-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: 6.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 576795839 610 VCQLCQEDDSLTK--NTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCH 657
Cdd:cd15760    7 RCDVCRKKFGLFKrrHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
622-657 7.02e-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: 7.02e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 576795839 622 KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCH 657
Cdd:cd15733   23 KHHCRNCGNVFCADCSNYKLPIPDEqlYDPVRVCNSCY 60
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
301-571 8.53e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 8.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   301 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEElavannRIITLQEEMERVKEESSYLLESNRKG 380
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   381 PKQDRTAEGQA----------LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQ 447
Cdd:TIGR02169  314 ERELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREK 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   448 LDDLralKHELAFKLQSSDLGVKQKSELNSRL----------EEKTNQMAATIKQLEQRLRQAERGRQSAELDnrlfKQD 517
Cdd:TIGR02169  394 LEKL---KREINELKRELDRLQEELQRLSEELadlnaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSK 466
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 576795839   518 FGDKINSLQLEVEALTRQRTQLELELKQ-EKERKSQNRGTPGKGAQKPELRMDGK 571
Cdd:TIGR02169  467 YEQELYDLKEEYDRVEKELSKLQRELAEaEAQARASEERVRGGRAVEEVLKASIQ 521
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
324-550 9.98e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 48.94  E-value: 9.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  324 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKgpkqDRTAEGQALSEARKHLKEET 403
Cdd:COG1196   300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLE-ELEQLLA----ELEEAKEELEEKLSALLEEL 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  404 QLRLDVEKElELQISMRQEMELAMKM--LEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEE 481
Cdd:COG1196   375 EELFEALRE-ELAELEAELAEIRNELeeLKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEE 453
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576795839  482 KTNQMAATIKQLEQRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEAL--TRQRTQLELELKQEKERK 550
Cdd:COG1196   454 QLEELRDRLKELERELAELQEELQRLE-----------KELSSLEARLDRLeaEQRASQGVRAVLEALESG 513
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
318-548 1.23e-05

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


Pssm-ID: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 48.63  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   318 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALS 393
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLEEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   394 EARKHLKEE-------TQLRL-------DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 459
Cdd:pfam01576  163 EFTSNLAEEeekvkslNKLKNkheamisDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAKKE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   460 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVE-ALTRQRTQ 538
Cdd:pfam01576  243 EELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRR----DLGEELEALKTELEdTLDSTAAQ 318
                          250
                   ....*....|
gi 576795839   539 LELELKQEKE 548
Cdd:pfam01576  319 QELRSKREQE 328
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
318-554 2.11e-05

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 47.83  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 318 EELNRHLNATVNNLQTKVDLLEKSNTKLtEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARK 397
Cdd:COG0419  318 EELLEKLKSLEERLEKLEEKLEKLESEL-EELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKE 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 398 HLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAL------------KHELAFKLQSS 465
Cdd:COG0419  397 ELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELagagekcpvcgqELPEEHEKELL 476
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 466 DLGVKQKSELNSRL--EEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELEL 543
Cdd:COG0419  477 ELYELELEELEEELsrEKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQ 556
                        250
                 ....*....|.
gi 576795839 544 KQEKERKSQNR 554
Cdd:COG0419  557 LKEELRQLEDR 567
PRK11281 PRK11281
mechanosensitive channel MscK;
317-539 2.15e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.98  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  317 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEESSY----------LLESNRKGPKQDR- 385
Cdd:PRK11281  123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  386 ------TAEgQALSEA-----RKHLKEETQL------RLDvekELELQISmRQEMELA----------MKMLEKDVCEKQ 438
Cdd:PRK11281  192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRD---YLTARIQ-RLEHQLQllqeainskrLTLSEKTVQEAQ 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  439 DALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERG--------RQSAELD 510
Cdd:PRK11281  267 SQDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLS 339
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 576795839  511 NRLFKQ-----------DFGDKINSLQLEVEALTRQRTQL 539
Cdd:PRK11281  340 RILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
611-657 3.00e-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: 3.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 576795839 611 CQLCQEDDSLTKNT--CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCH 657
Cdd:cd15749    2 CFGCAAKFSLFKKEcgCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
313-502 3.35e-05

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 46.94  E-value: 3.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 313 QKNYV--EELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQ 390
Cdd:COG4372  129 RQNLAkaQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATR 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 391 AlsEARKHLKEETQLRLDVEKELELQISMR----QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS- 465
Cdd:COG4372  209 A--NAAQARTEELARRAAAAQQTAQAIQQRdaqiSQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYv 286
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 576795839 466 DLGVKQKSELNSRLE----EKTNQMAATIKQLEQRLRQAER 502
Cdd:COG4372  287 RLRQQAAATQRGQVLagaaQRVAQAQAQAQAQAQLLSSANR 327
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
622-662 3.83e-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: 3.83e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 576795839 622 KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIK 662
Cdd:cd15739   26 KHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
318-552 6.80e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 6.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  318 EELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEG-------- 389
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikelekq 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  390 -------------QALSEARKHLKEETQLRLDVEKELELQISMRQ----EMELAMKMLEKDVCEKQDALVSLRQQL---- 448
Cdd:TIGR04523 290 lnqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  449 DDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMaatiKQLEQRLRQAERGRQSAELDNRLFKQDfgdkINSLQLE 528
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKET----IIKNNSE 441
                         250       260
                  ....*....|....*....|....
gi 576795839  529 VEALTRQRTQLELELKQEKERKSQ 552
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRES 465
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
327-587 8.41e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 8.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 327 TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgqalSEARKHLKEETQLR 406
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 407 L-DVEKELELQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 485
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 486 MAATIKQLEQRLRQAErgrqsaELDNRLFKQDfgDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGTPGKgaQKPE 565
Cdd:PRK03918 537 LKGEIKSLKKELEKLE------ELKKKLAELE--KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN--EYLE 606
                        250       260
                 ....*....|....*....|..
gi 576795839 566 LRmDGKHRIQEENVKLKKPLEE 587
Cdd:PRK03918 607 LK-DAEKELEREEKELKKLEEE 627
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
610-660 9.90e-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: 9.90e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 610 VCQLCQEDDSLTKNT---CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCHEQL 660
Cdd:cd15755   10 VCMRCQKAKFTPVNRrhhCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
309-552 9.92e-05

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 45.52  E-value: 9.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 309 AILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLES-NRKGPKQDRTA 387
Cdd:COG0419  484 EELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKlQLQQLKEELRQ 563
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 388 EGQALSEARKHLKEETQLRLDVEKELELQISMRQ----EMELAMKMLEK----DVCEKQDALVSLRQQLDDLRALKHELA 459
Cdd:COG0419  564 LEDRLQELKELLEELRLLRTRKEELEELRERLKElkkkLKELEERLSQLeellQSLELSEAENELEEAEEELESELEKLN 643
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 460 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEALTR 534
Cdd:COG0419  644 LQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQlreelEELLKKLGEIEQLIEELES 723
                        250
                 ....*....|....*...
gi 576795839 535 QRTQLElELKQEKERKSQ 552
Cdd:COG0419  724 RKAELE-ELKKELEKLEK 740
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
319-496 1.18e-04

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


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 45.06  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 319 ELNRhLNATVNNLQTKVDLL--------------EKSNTKLTEELAVANNRIITLQEEMERVKEesSYLLesnrkgpkqd 384
Cdd:COG4477  275 ELDE-AEEELGLIQEKIESLydllereveaknvvEENLPILPDYLEKAKENNEHLKEEIERVKE--SYRL---------- 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 385 rtAEGQALSEAR--KHLKEETQLRLDVEKELELQ-------ISMRQEMELAMKMLEKDVCEKQDALVSLR-------QQL 448
Cdd:COG4477  342 --AETELGSVRKfeKELKELESVLDEILENIEAQevayselQDNLEEIEKALTDIEDEQEKVQEHLTSLRkdelearENL 419
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 576795839 449 DDLRALKHELAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 496
Cdd:COG4477  420 ERLKSKLHEIKRYMEKSNLpGLPE--TFLSLFFTAGHEIQDLMKELSEV 466
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
306-612 1.18e-04

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: 45.34  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   306 QITAILDQknyvEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMErvkeessyLLESNRKGPKQDR 385
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAE--------LCAAAITCTAQCE 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   386 TAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEME---LAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL 462
Cdd:TIGR00618  455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   463 QSSDLGVKQKSELNSRLEEKTNQmAATIKQLEQRLRQAE------RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQR 536
Cdd:TIGR00618  535 QTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFsiltqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839   537 TQLELELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEEnvkLKKPLEESHRLLTHPAEEQGQPSLSEKPQVCQ 612
Cdd:TIGR00618  614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT---LTQERVREHALSIRVLPKELLASRQLALQKMQ 686
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
308-481 1.45e-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: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  308 TAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRkgpkqDRTA 387
Cdd:COG1196   351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLE-----DLKE 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  388 EGQALSEARKHLKEETQLRLDVEKELELQISMRQEmelAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 467
Cdd:COG1196   426 ELKELEAELEELQTELEELNEELEELEEQLEELRD---RLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
                         170
                  ....*....|....
gi 576795839  468 GVKQKSELNSRLEE 481
Cdd:COG1196   503 VRAVLEALESGLPG 516
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
315-509 2.02e-04

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 44.04  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 315 NYVEELNRHLNATVNNLQTKVDLlEKSNTKLTEELAvANNRIITLQEEMERVKE-ESSYLLESNRKGPKQDRTAEGQALS 393
Cdd:COG4487    2 KEIKVPIQTKPFTIPKCEDSIKG-EQARYKQIEQED-QSRILNTLEEFEKEANEkRAQYRSAKKKELSQLEEQLINQKKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 394 EARKHLKEETQLRLDVEKE---LELQISMRQEMELAMKMLEKDVCEKQDALVSL-----------RQQLDDLRALKHELA 459
Cdd:COG4487   80 QKNLFNEQIKQFELALQDEiakLEALELLNLEKDKELELLEKELDELSKELQKQlqntaeiiekkRENNKNEERLKFENE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576795839 460 FKLQSSDLGVKQKSElnSRLEEKTNQM--AATIKQLEQRLRQAERGRQSAEL 509
Cdd:COG4487  160 KKLEESLELEREKFE--EQLHEANLDLefKENEEQRESKWAILKKLKRRAEL 209
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
334-501 2.04e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  334 KVDLLEKSNTKLTEELAVANNRIITLQE----------------EMERVKEES---SYLLESNRKGPKQDRTAEGQALSE 394
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  395 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQK 472
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKA 561
                         170       180       190
                  ....*....|....*....|....*....|.
gi 576795839  473 SELNSRLE--EKTNQMAATIKQLEQRLRQAE 501
Cdd:pfam17380 562 TEERSRLEamEREREMMRQIVESEKARAEYE 592
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
382-587 2.24e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.71  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  382 KQDRTAEGQALSEARKHLKEetqLRLDVEKELELQISMRQEMELAMKMLEKdvcekqdalvsLRQQLDDLRALKHELAFK 461
Cdd:COG1196   659 KRSSLAQKRELKELEEELAE---LEAQLEKLEEELKSLKNELRSLEDLLEE-----------LRRQLEELERQLEELKRE 724
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  462 LQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEALTRQRTQLEL 541
Cdd:COG1196   725 LAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLE-----------EALAKLKEEIEELEEKRQALQE 793
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 576795839  542 ELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEENVKLKKPLEE 587
Cdd:COG1196   794 ELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEE 839
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
313-458 2.58e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   313 QKNYVEELNRH--LNATVNNLQTKVDLLEKSNT-------KLTEELAVANNRIITLQEEMERvkeessylLESNRKGPKQ 383
Cdd:TIGR02168  350 KEELESLEAELeeLEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLER--------LEDRRERLQQ 421
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839   384 DRTAEGQALSEARkhlKEETQLRLD-VEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 458
Cdd:TIGR02168  422 EIEELLKKLEEAE---LKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
mukB PRK04863
chromosome partition protein MukB;
392-554 2.91e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  392 LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 469
Cdd:PRK04863  444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  470 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAErGRQSAELDNRLFKQDF----GDKINSLQLEVEALTRQRTQLELELK 544
Cdd:PRK04863  519 RMRlSELEQRLRQQ--------QRAERLLAEFC-KRLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589
                         170
                  ....*....|
gi 576795839  545 QEKERKSQNR 554
Cdd:PRK04863  590 QLQARIQRLA 599
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
313-609 3.27e-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: 43.75  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 313 QKNYVEELnRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRiitLQEEMERVKEESSYLLESNRKGPKQDRTAEgqal 392
Cdd:NF033930 103 QKAYVKYR-KAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAE---FNKVRAKVVPEAEELAETKKKAEEAKAEEP---- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 393 sEARKHLKEETQLRLDVEKELElqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG--VK 470
Cdd:NF033930 175 -VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSEdyIK 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 471 Q--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEK 547
Cdd:NF033930 243 EglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSDNNVA 322
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576795839 548 ERKSQnrgtpgkGAQKPelRMDGKHRIQEENVKLKKPLEEshrlLTHPAEEQGQPSLSEKPQ 609
Cdd:NF033930 323 DYYKE-------ALEKD--LATKKAELEKTQKDLDKALNE----LGPDGDEEETPAPAPQPE 371
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
331-500 3.36e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 43.89  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  331 LQTKVDLLEKSNTKLTE-----ELAVANNRIITLQEEMERVKEESSYLLESNRKGPkqdrTAEGQALSEARKhlKEETQL 405
Cdd:PRK10929  112 LQVSSQLLEKSRQAQQEqdrarEISDSLSQLPQQQTEARRQLNEIERRLQTLGTPN----TPLAQAQLTALQ--AESAAL 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  406 RLDVEkELEL-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL------QSSDL--GVKQKS 473
Cdd:PRK10929  186 KALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEStellaeQSGDLpkSIVAQF 264
                         170       180
                  ....*....|....*....|....*..
gi 576795839  474 ELNSRLEEKTNQMAATIKQLEQRLRQA 500
Cdd:PRK10929  265 KINRELSQALNQQAQRMDLIASQQRQA 291
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
310-542 6.20e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 6.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   310 ILDQK--NYVEELnRHLNATVNNLQTKVDLLEKSNTKLTEELAvaNNRIITLQEEMERVKEESSYLLESNR--KGPKQDR 385
Cdd:TIGR02169  748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLReiEQKLNRL 824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   386 TAEGQALSEARKHLKE---ETQLRL-DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFK 461
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEqriDLKEQIkSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   462 LQssdlgvKQKSELNsRLEEKTNQMAATIKQLEQRLRQAErgrqsaeldnRLFKQDFGDKINSLQLEVEALTRQRTQLEL 541
Cdd:TIGR02169  905 IE------ELEAQIE-KKRKRLSELKAKLEALEEELSEIE----------DPKGEDEEIPEEELSLEDVQAELQRVEEEI 967

                   .
gi 576795839   542 E 542
Cdd:TIGR02169  968 R 968
YloA COG1293
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ...
420-583 6.94e-04

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: 42.76  E-value: 6.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 420 RQEMELAMKMLEKDVC---EKQDALVSLRQqLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQR 496
Cdd:COG1293  230 REALEELLNPLKPNYYykdEKYLDVVPLKA-YADLEKLFNEALDEKFERDKIKQLASELEKKLEKELKKLENKLEKQEDE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 497 LRQAERgrqsaeLDNRLFKQdfGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGTPGKGAQ---KPELRMDGKHR 573
Cdd:COG1293  309 LEELEK------AAEELRQK--GELLYANLQLIEEGLKSVRLADFYGNEEIKIELDKSKTPSENAQryfKKYKKLKGAKV 380
                        170
                 ....*....|
gi 576795839 574 IQEENVKLKK 583
Cdd:COG1293  381 NLDRQLSELK 390
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
611-656 7.47e-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: 7.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 576795839 611 CQLCQEDDS--LTKNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPC 656
Cdd:cd15726   10 CLDCKSEFSwmVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
611-656 7.85e-04

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 37.87  E-value: 7.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKP--ERVCNPC 656
Cdd:cd15745    2 CAICAKAFSLFrrKYVCRLCGGVVCHSCSSEDLVLSVPDTCiyLRVCKTC 51
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
318-555 8.12e-04

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


Pssm-ID: 318193 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 8.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   318 EELNRHLNATVNNLQT----KVDLLEKSNTKLtEELavannRIITLQEEmERVKEESSYLLE----SNRKGPKQDRTAE- 388
Cdd:pfam15921  141 EDLRNQLQNTVHELEAakclKEDMLEDSNTQI-EQL-----RKMMLSHE-GVLQEIRSILVDfeeaSGKKIYEHDSMSTm 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   389 -----GQALSEARKHLKEETQLR----LDVEKELE-LQISMRQEMELAMKM----LEKDVCEKQDALVSLRQQLDDLRAL 454
Cdd:pfam15921  214 hfrslGSAISKILRELDTEISYLkgriFPVEDQLEaLKSESQNKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARSQ 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   455 KHELAFKLQssdLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSA--ELDNRL----------------FKQ 516
Cdd:pfam15921  294 ANSIQSQLE---IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKieELEKQLvlanseltearterdqFSQ 370
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 576795839   517 DFGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRG 555
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG 409
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
310-597 8.96e-04

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: 42.57  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  310 ILDQKNYV-EELNRHLNATVNNLQTKVDLlEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAE 388
Cdd:COG3096   263 ISEATNYVaADYMRHANERRVHLDQALEF-RRELYTSRQQLAAEQYRHVDMSRELAELNGAEG-DLEADYQAASDHLNLV 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  389 GQALSEARKHLK-----EETQLRLDVEKELELQISMRQ-EMELAMKMLEKDVCEKQDALVSLRQQLD--DLRALKHELAF 460
Cdd:COG3096   341 QTALRQQEKIERyqadlEELTIRLEEQNEVVEEANERQeENEARAEAAELEVDELKSQLADYQQALDvqQTRAIQYQQAI 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  461 K--------LQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGdkinslqlEVEAL 532
Cdd:COG3096   421 AalerakelCHLPDLTADSAEEWLETFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAG--------ELARS 492
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795839  533 TRQRTQLELeLKQEKERKSQNRGTPGKGAQKPELrmDGKHRIQEENVKLKKPLEESHRLLTHPAE 597
Cdd:COG3096   493 EAWDVAREL-LREGPDQRHLAEQVQPLRMRLSEL--EQRLRQQQSAERLLADFCKRQGKNLDAEE 554
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
310-552 1.07e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 310 ILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIitlqEEMERVKEESSYLLESNRKGPKQDRTAEg 389
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLE- 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 390 QALSEARKHLkEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGV 469
Cdd:PRK03918 259 EKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 470 KQKSELNSRLEEKTNQMAAtikqLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKER 549
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413

                 ...
gi 576795839 550 KSQ 552
Cdd:PRK03918 414 IGE 416
CCDC154 pfam15450
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ...
399-626 1.10e-03

Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.


Pssm-ID: 406016 [Multi-domain]  Cd Length: 526  Bit Score: 42.12  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  399 LKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCE-KQDALVSLRQQLDDLRALKHELAFKLQssdlgvKQKSELNS 477
Cdd:pfam15450  47 LRELAQLRASMQLQDSELQDLRQEVQQPAKEPEKEAGEfNGPQNQNQMQALDKRLVEVREALTQIR------RKQALQDS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  478 RLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINslqLEVEALTRQRTQLELE-LKQEKERKSQNRGT 556
Cdd:pfam15450 121 ERKGASQEAALRLGKLTGMLKQEEQAREAACSSLQKSQEEASQKVD---REVARMQAQGTKLGEEmSLRFLKREAKLCGF 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576795839  557 pgkgAQKPELRMDGKHRIQEEN-VKLKKPLEESHRLLTHPAEEQGQPSLSekpQVCQLCQEDDSLTKNTCR 626
Cdd:pfam15450 198 ----LQKSFLALEKRMKASESArLSLEGELREELERRWQLLQELAEERLR---ALEGQEEQEEEHLLEQCR 261
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
605-660 1.66e-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: 1.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 576795839 605 SEKPQvCQLCQEDDSLTK--NTCRNCRGTFCNACTTNELPLPS-SIKPERVCNPCHEQL 660
Cdd:cd15729   11 SEAPN-CMQCEVKFTFTKrrHHCRACGKVLCSACCSLKARLEYlDNKEARVCVPCYQTL 68
YhaN COG4717
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
343-562 1.92e-03

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


Pssm-ID: 227061 [Multi-domain]  Cd Length: 984  Bit Score: 41.37  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 343 TKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELelqismRQE 422
Cdd:COG4717  277 EKREAHLQKTEAEIDALLVRLAELKDLAS-QLIPAKEAVLQALVRLHQQLSEIKASAFELTETLAGIEADL------RDK 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 423 MELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAfklqssdlgvkqksELNSRLEEKTNQMAATIKQLEQRLRQAE- 501
Cdd:COG4717  350 EEAAGNGFEAERVHDLRSLECMLRYQSSQRELKQTEA--------------AYCKRLDEKRLFEDEAEEEARQRLADDEe 415
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839 502 --RGRQSAELDNRLFKQDFGDKINSLQLEVEALT---RQRTQLELELKQEKERKSQNRGTPGKGAQ 562
Cdd:COG4717  416 evRAGDEAREEKIAANSQVIDKEEVCNLYDRRDTawqKQRFLREKQTAFERQKTEHTKIIALRLAG 481
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
622-657 1.98e-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: 1.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 576795839 622 KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCH 657
Cdd:cd15738   24 KHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
317-496 2.20e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.97  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 317 VEELNRHLNATVNNLqtkVDLLE----------KSNTKLTEELAVANNRIITLQEEMERVKEesSYLL-----ESNRKGP 381
Cdd:PRK04778 280 AEEKNEEIQERIDQL---YDILErevkarkyveKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTLneselESVRQLE 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 382 KQ------------DRTAEG-QALSEARKHLKE-ETQLRlDVEKElelQISMRQEmelaMKMLEKDvcEKQdalvsLRQQ 447
Cdd:PRK04778 355 KQleslekqydeitERIAEQeIAYSELQEELEEiLKQLE-EIEKE---QEKLSEM----LQGLRKD--ELE-----AREK 419
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 576795839 448 LDDLRALKHELAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 496
Cdd:PRK04778 420 LERYRNKLHEIKRYLEKSNLpGLPE--DYLEMFFEVSDEIEALAEELEEK 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
343-554 4.40e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   343 TKLTEELAVANNRIITLQEEMERVKEessYLLESNRKGPKQDRTAEgqaLSEARKHLKEE-TQLRLDVE-KELELQISMR 420
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLED---ILNELERQLKSLERQAE---KAERYKELKAElRELELALLvLRLEELREEL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   421 QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS--SDLG--VKQKSELNSRLEEKTNQMAATIKQLEQR 496
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqKELYalANEISRLEQQKQILRERLANLERQLEEL 321
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 576795839   497 LRQAERGRQSAELDNRLFKQdFGDKINSLQLEVEALtrqRTQLELELKQEKERKSQNR 554
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAE-LEEKLEELKEELESL---EAELEELEAELEELESRLE 375
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
360-607 4.57e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.11  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  360 QEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARKHLKEEtqlRLDVEKELELQiSMRQE-----------MELAMK 428
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE---RMAMERERELE-RIRQEerkrelerirqEEIAME 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  429 M-----LEKDVCEKQDALVSLRQQLDDLRALK---HELAFKLQssdlgvKQKSELNSRLEEKTNQMAATIKQLEQ-RLRQ 499
Cdd:pfam17380 374 IsrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQ------QQKVEMEQIRAEQEEARQREVRRLEEeRARE 447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  500 AERGRQsaeldnrlfkqdfgdkinslqlevEALTRQRtQLELELKQEKERKSQnrgtpgKGAQKPELRmdGKHRIQEENV 579
Cdd:pfam17380 448 MERVRL------------------------EEQERQQ-QVERLRQQEEERKRK------KLELEKEKR--DRKRAEEQRR 494
                         250       260
                  ....*....|....*....|....*....
gi 576795839  580 K-LKKPLEESHRLLThpaEEQGQPSLSEK 607
Cdd:pfam17380 495 KiLEKELEERKQAMI---EEERKRKLLEK 520
CwlO1 COG3883
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
293-500 5.02e-03

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


Pssm-ID: 226400 [Multi-domain]  Cd Length: 265  Bit Score: 39.32  E-value: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 293 KDGNSSKGSEGDGQITAIL-DQKNYVEELNRhLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKE--- 368
Cdd:COG3883   26 AALLSDKIQNQDSKLSELQkEKKNIQNEIES-LDNQIEEIQSKIDELQKEIDQSKAEIKKLQKEIAELKENIVERQEllk 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 369 -----------ESSYL---LESNRKGPKQDR-TAEGQALSEARKHLK--EETQLRL-----DVEKELELQISMRQEMELA 426
Cdd:COG3883  105 kraramqvngtATSYIdviLNSKSFSDLISRvTAISVIVDADKKILEqqKEDKKSLeekqaALEDKLETLVALQNELETQ 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 427 MKMLEKDVCEKQDALVSLRQQLDDLRALKHELafklqssdlgVKQKS-ELNSRLEEKTNQMAATIKQLEQRLRQA 500
Cdd:COG3883  185 LNSLNSQKAEKNALIAALAAKEASALGEKAAL----------EEQKAlAEAAAAEAAKQEAAAKAAAQEQAALQA 249
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
323-372 6.59e-03

Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a family of proteins with a predicted coiled-coil domain conserved from nematodes to humans. It carries a characteristic TTKRSYEDQ sequence-motif. The function is not known.


Pssm-ID: 402010  Cd Length: 523  Bit Score: 39.42  E-value: 6.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 576795839  323 HLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKeeSSY 372
Cdd:pfam10212 443 HFHAECRALAKRLALAEKSKESLTEELKLANQNISRLQDELTTTK--RSY 490
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
324-552 6.94e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 39.78  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  324 LNATVNnlQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESnrkgpKQDRTAEGQALSEA---RKHLK 400
Cdd:PRK10246  523 LEPGVN--QSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE-----EQALTQQWQAVCASlniTLQPQ 595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  401 EETQLRLDVEKELELQ---ISMRQEMELAMKMLEKDVCEKQDALVSLRQQL-DDLRALKHE----------LAFKLQSSD 466
Cdd:PRK10246  596 DDIQPWLDAQEEHERQlrlLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLlTALAGYALTlpqedeeaswLATRQQEAQ 675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  467 LGVKQKSELNsRLEEKTNQMAATIKQLEQRlRQAERGRQSAELDNRlfkQDFGDKINSLQLEVEALTRQRTqlelelkQE 546
Cdd:PRK10246  676 SWQQRQNELT-ALQNRIQQLTPLLETLPQS-DDLPHSEETVALDNW---RQVHEQCLSLHSQLQTLQQQDV-------LE 743

                  ....*.
gi 576795839  547 KERKSQ 552
Cdd:PRK10246  744 AQRLQK 749
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
318-509 7.77e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 318 EELNRHLNATVNNLQTKVDLLEKSntklTEELAVANNRIITLQEEMERVKEESSYLL-ESNRKGPKQDRTAEGQaLSEAR 396
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLkELEELGFESVEELEER-LKELE 598
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 397 KHLKEETQLRlDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKlQSSDLGVKQKSELN 476
Cdd:PRK03918 599 PFYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE-ELREEYLELSRELA 676
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 576795839 477 S------RLEEKTNQMAATIKQLEQRLRQAERGRQSAEL 509
Cdd:PRK03918 677 GlraeleELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
327-552 9.09e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  327 TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESsyllesnrKGPKQDRTAEGQALSEARKHLKEETQLR 406
Cdd:TIGR04523  69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI--------KNDKEQKNKLEVELNKLEKQKKENKKNI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  407 LDV-------EKELELQ-------ISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDL--------------RALKHEL 458
Cdd:TIGR04523 141 DKFlteikkkEKELEKLnnkyndlKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnlkkkiqknKSLESQI 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  459 A-FKLQSSDLGvKQKSELNSRLEEKTNQMAATIKQLEQRL-------RQAERGRQSAELDNRLFKQdFGDKINSLQLEVE 530
Cdd:TIGR04523 221 SeLKKQNNQLK-DNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikKQLSEKQKELEQNNKKIKE-LEKQLNQLKSEIS 298
                         250       260
                  ....*....|....*....|....*..
gi 576795839  531 ALTRQRTQ-----LELELKQEKERKSQ 552
Cdd:TIGR04523 299 DLNNQKEQdwnkeLKSELKNQEKKLEE 325
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
323-512 9.27e-03

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 38.12  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 323 HLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALSEArKHLKEE 402
Cdd:COG1579   14 KLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAE-EKLSAV-KDEREL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 403 TQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEK 482
Cdd:COG1579   92 RALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSKREELKEK 171
                        170       180       190
                 ....*....|....*....|....*....|
gi 576795839 483 TNQMAATIKqleQRLRQAERGRQSAELDNR 512
Cdd:COG1579  172 LDPELLSEY---ERIRKNKKGVGVVPLEGR 198
HEC1 COG5185
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ...
338-626 9.44e-03

Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227512 [Multi-domain]  Cd Length: 622  Bit Score: 39.19  E-value: 9.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 338 LEKSNTKLTEELAVANNRIIT-LQEEMERVKEESSYLLEsnrkgpkqdRTAEGQALSEARKHLKEETQLRLDVEKELELQ 416
Cdd:COG5185  247 LEDNYEPSEQELKLGFEKFVHiINTDIANLKTQNDNLYE---------KIQEAMKISQKIKTLREKWRALKSDSNKYENY 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 417 IS-MRQEMEL---AMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQ 492
Cdd:COG5185  318 VNaMKQKSQEwpgKLEKLKSEIELKEEEIKALQSNIDELHKQLRKQGISTEQFELMNQEREKLTRELDKINIQSDKLTKS 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 493 LEQRLRQAERGRQSAEldnRLFkQDFGDKINSLQLEVEALTRQRTQLELELKQEkerKSQNRGTPGKGAQKP---ELRMD 569
Cdd:COG5185  398 VKSRKLEAQGIFKSLE---KTL-RQYDSLIQNITRSRSQIGHNVNDSSLKINIE---QLFPKGSGINESIKKsilELNDE 470
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576795839 570 GKHRIQEE---NVKLKKPLEESHRLLTHPAEEQGQPS--LSEKPQVCQLCQEDDSLTKNTCR 626
Cdd:COG5185  471 IQERIKTEenkSITLEEDIKNLKHDINELTQILEKLEleLSEANSKFELSKEENERELVAQR 532
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
326-549 9.51e-03

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


Pssm-ID: 401982 [Multi-domain]  Cd Length: 765  Bit Score: 39.04  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  326 ATVNNLQTKVDLLEKSNTKLTEELAVANN------RIITLQEEMERVKEESSYLLESNRkgpkqDRTAEGQALSEARKHL 399
Cdd:pfam10174 191 MQLGHLEVLLDQKEKENIHLREELHRRNQlqpdpaKTKALQTVIEMKDTKISSLERNIR-----DLEDEVQMLKTNGLLH 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  400 KEETQLRLdveKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDL-----------RALKHELAFKLQSSDLG 468
Cdd:pfam10174 266 TEDREEEI---KQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLtnqnsdckqhiEVLKESLTAKEQRAAIL 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  469 VKQKSELNSRLEEKTNQMAATIKQLeQRLrQAERGRQSAELDNRLFKQDFGD-KINSLQLEVEALTRQRTQLELELKQEK 547
Cdd:pfam10174 343 QTEVDALRLRLEEKESFLNKKTKQL-QDL-TEEKSTLAGEIRDLKDMLDVKErKINVLQKKIENLQEQLRDKDKQLAGLK 420

                  ..
gi 576795839  548 ER 549
Cdd:pfam10174 421 ER 422
 
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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