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Conserved domains on  [gi|545521739|ref|XP_005628330|]
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Protein Classification

RUN and FYVE_RUFY3 domain-containing protein (domain architecture ID 13681830)

protein containing domains RUN, DUF460, XseA, 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 ...
121-242 8.47e-45

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


:

Pssm-ID: 397055  Cd Length: 129  Bit Score: 155.50  E-value: 8.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  121 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 194
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 545521739  195 SEYMKALINKKELLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCM 242
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
579-626 5.93e-20

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


:

Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 83.24  E-value: 5.93e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 545521739 579 ICQLCQEDG---SLTKNVCKNCRGTFCNACSTNELPLPSSI-KPERVCNPCH 626
Cdd:cd15744    1 SCSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-523 1.72e-09

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   261 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 337
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   338 SSyILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 417
Cdd:TIGR02168  735 LA-RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   418 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 497
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*.
gi 545521739   498 EELTRQRHQLELELKQERERRLQNNR 523
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRR 915
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
121-242 8.47e-45

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 397055  Cd Length: 129  Bit Score: 155.50  E-value: 8.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  121 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 194
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 545521739  195 SEYMKALINKKELLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCM 242
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
579-626 5.93e-20

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 83.24  E-value: 5.93e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 545521739 579 ICQLCQEDG---SLTKNVCKNCRGTFCNACSTNELPLPSSI-KPERVCNPCH 626
Cdd:cd15744    1 SCSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
181-243 2.06e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 79.19  E-value: 2.06e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545521739   181 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 243
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
573-629 7.75e-10

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


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 55.13  E-value: 7.75e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545521739   573 PSEKPQICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPCHEHL 629
Cdd:smart00064   6 PDEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-523 1.72e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   261 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 337
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   338 SSyILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 417
Cdd:TIGR02168  735 LA-RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   418 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 497
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*.
gi 545521739   498 EELTRQRHQLELELKQERERRLQNNR 523
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRR 915
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
271-525 1.98e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.88  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  271 GDGQITAILDQKNYVEELNRHL---NATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRK 347
Cdd:COG1196   655 GSRNKRSSLAQKRELKELEEELaelEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELA-ALEEELE 733
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  348 GPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 427
Cdd:COG1196   734 QLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALE 813
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  428 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAE---LDNRLFKQDFGDKINSLQLEVEELTRQR 504
Cdd:COG1196   814 RELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKeelEELEAEKEELEDELKELEEEKEELEEEL 893
                         250       260
                  ....*....|....*....|.
gi 545521739  505 HQLELELKQERERRLQNNRSI 525
Cdd:COG1196   894 RELESELAELKEEIEKLRERL 914
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
580-631 2.13e-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: 51.23  E-value: 2.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 545521739  580 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSI---KPERVCNPCHEHLMK 631
Cdd:pfam01363  12 CMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTLQK 68
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
277-578 1.22e-06

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: 51.45  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 277 AILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyilESNRKGPkqdrtse 356
Cdd:NF033930 105 AYVKYRKAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAEFNKVRAKVVPEAEELAETKKKAE---EAKAEEP------- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 357 gqalsEARKHLKEETQLRLDVEKELEiqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG 436
Cdd:NF033930 175 -----VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 437 --VKQ--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RGRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELEL 511
Cdd:NF033930 239 dyIKEglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSD 318
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545521739 512 KQERERRLQnnrsipgkGSQKpePKTDGKHKIQEENVKLKKPLDEshrlPSRPVDGQDQPPPSEKPQ 578
Cdd:NF033930 319 NNVADYYKE--------ALEK--DLATKKAELEKTQKDLDKALNE----LGPDGDEEETPAPAPQPE 371
PRK11281 PRK11281
mechanosensitive channel MscK;
285-507 5.90e-06

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 49.52  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  285 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVKEESSY----------ILESNRKGPKQDRT 354
Cdd:PRK11281  123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRP 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  355 SE------GQALSEA-----RKHLKEETQL------RLDvEKELEIQismRQEMELA----------MKMLEKDVCEKQD 407
Cdd:PRK11281  192 SQrvllqaEQALLNAqndlqRKSLEGNTQLqdllqkQRD-YLTARIQ---RLEHQLQllqeainskrLTLSEKTVQEAQS 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  408 ALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERG--------RQSAELDN 479
Cdd:PRK11281  268 QDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLSR 340
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 545521739  480 RLFKQ-----------DFGDKINSLQLEVEELTRQRHQL 507
Cdd:PRK11281  341 ILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
328-560 8.49e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  328 QEEMERVKEESSYILESNRKGPKQDRTSEGQALSEARKHLKEEtQLRLDVEKELE-IQIS--------MRQEmELAMKM- 397
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE-RMAMERERELErIRQEerkrelerIRQE-EIAMEIs 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  398 ----LEKDVCEKQDALVSLRQQLDDLRALK-----HELAFKLQSSDLGVKQKSELNSR------LEEKTNQMAATIKQLE 462
Cdd:pfam17380 376 rmreLERLQMERQQKNERVRQELEAARKVKileeeRQRKIQQQKVEMEQIRAEQEEARqrevrrLEEERAREMERVRLEE 455
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  463 Q-RLRQAERGRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRHQLELELKQERERRLQNNRSIPGKGSQKPEPKT--DG 539
Cdd:pfam17380 456 QeRQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEE 533
                         250       260
                  ....*....|....*....|.
gi 545521739  540 KHKIQEENVKLKKPLDESHRL 560
Cdd:pfam17380 534 RRREAEEERRKQQEMEERRRI 554
M_group_A_cterm NF033777
M protein C-terminal domain; M protein (emm) is an important virulence protein and ...
336-474 3.04e-03

M protein C-terminal domain; M protein (emm) is an important virulence protein and serology-defining surface antigen of Streptococcus pyogenes (group A Streptococcus). M protein has an amino-terminal YSIRK-type signal sequence (associated with cross-wall targeting in dividing cells), and a C-terminal LPXTG domain for processing by sortase and covalent attachment to the Gram-positive cell wall. Past the signal peptide, M protein has a hypervariable region, but this HMM describes only the well-conserved region C-terminal to the hypervariable region. It discriminates M protein from two related proteins, Enn and Mrp.


Pssm-ID: 411361 [Multi-domain]  Cd Length: 218  Bit Score: 39.43  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 336 EESSYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ 415
Cdd:NF033777   8 EEQNKISEASRKGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSK 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545521739 416 LDDLRALKHELAfklQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQS 474
Cdd:NF033777  88 LAALEKLNKELE---ESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAGKAS 143
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
121-242 8.47e-45

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 397055  Cd Length: 129  Bit Score: 155.50  E-value: 8.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  121 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 194
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 545521739  195 SEYMKALINKKELLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCM 242
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
579-626 5.93e-20

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 83.24  E-value: 5.93e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 545521739 579 ICQLCQEDG---SLTKNVCKNCRGTFCNACSTNELPLPSSI-KPERVCNPCH 626
Cdd:cd15744    1 SCSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
181-243 2.06e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 79.19  E-value: 2.06e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545521739   181 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 243
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
580-626 2.26e-16

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277261 [Multi-domain]  Cd Length: 58  Bit Score: 73.57  E-value: 2.26e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 545521739 580 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPCH 626
Cdd:cd15721   10 CQQCEKEFSLSrrKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
580-636 6.19e-14

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


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 66.97  E-value: 6.19e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545521739 580 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPCHEHLMKQYSSS 636
Cdd:cd15759   13 CKLCEKEFSLSkrKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
580-634 1.89e-13

FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277297 [Multi-domain]  Cd Length: 71  Bit Score: 65.47  E-value: 1.89e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 545521739 580 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPCHEHLMKQYS 634
Cdd:cd15758   15 CKQCEKEFSISrrKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
580-626 6.02e-10

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


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 54.85  E-value: 6.02e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 545521739 580 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPS--SIKPERVCNPCH 626
Cdd:cd00065    2 CMLCGKKFSLFrrRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
573-629 7.75e-10

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


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 55.13  E-value: 7.75e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545521739   573 PSEKPQICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPCHEHL 629
Cdd:smart00064   6 PDEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-523 1.72e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   261 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 337
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   338 SSyILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 417
Cdd:TIGR02168  735 LA-RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   418 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 497
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*.
gi 545521739   498 EELTRQRHQLELELKQERERRLQNNR 523
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRR 915
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
271-525 1.98e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.88  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  271 GDGQITAILDQKNYVEELNRHL---NATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRK 347
Cdd:COG1196   655 GSRNKRSSLAQKRELKELEEELaelEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELA-ALEEELE 733
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  348 GPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 427
Cdd:COG1196   734 QLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALE 813
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  428 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAE---LDNRLFKQDFGDKINSLQLEVEELTRQR 504
Cdd:COG1196   814 RELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKeelEELEAEKEELEDELKELEEEKEELEEEL 893
                         250       260
                  ....*....|....*....|.
gi 545521739  505 HQLELELKQERERRLQNNRSI 525
Cdd:COG1196   894 RELESELAELKEEIEKLRERL 914
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
290-517 3.14e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.11  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  290 RHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTSEGQA--LSEARKHL 367
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  368 KEETQLRLDVEKELEIQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 446
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  447 LEEKTNQMA---ATIKQLEQRL-----RQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEELTRQRHQLELELKQ 513
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELAE 471

                  ....
gi 545521739  514 ERER 517
Cdd:COG1196   472 LQEE 475
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
276-516 3.45e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.11  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  276 TAILDQKNYVEELNRHLNA---TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI------LESNR 346
Cdd:COG1196   688 EELKSLKNELRSLEDLLEElrrQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEEL 767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  347 KGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 426
Cdd:COG1196   768 ESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  427 AFKLQSSDlgvKQKSELNSRLEEKTNQMA----------ATIKQLEQRLRQAERGRQSAELDNrlfkQDFGDKINSLQLE 496
Cdd:COG1196   848 EEELEELE---KELEELKEELEELEAEKEeledelkeleEEKEELEEELRELESELAELKEEI----EKLRERLEELEAK 920
                         250       260
                  ....*....|....*....|
gi 545521739  497 VEELTRQRHQLELELKQERE 516
Cdd:COG1196   921 LERLEVELPELEEELEEEYE 940
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
579-626 1.14e-08

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


Pssm-ID: 277274 [Multi-domain]  Cd Length: 59  Bit Score: 51.76  E-value: 1.14e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 545521739 579 ICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLP--SSIKPERVCNPCH 626
Cdd:cd15735    8 VCMRCRTAFTFTnrKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
269-520 1.51e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.80  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  269 SEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESnrkg 348
Cdd:COG1196   719 EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE---- 794
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  349 pkqdRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAlkhelaf 428
Cdd:COG1196   795 ----LEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKE------- 863
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  429 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQdfgdKINSLQLEVEELTRQ-RHQL 507
Cdd:COG1196   864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEA----KLERLEVELPELEEElEEEY 939
                         250
                  ....*....|...
gi 545521739  508 ELELKQERERRLQ 520
Cdd:COG1196   940 EDTLETELEREIE 952
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
580-631 2.13e-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: 51.23  E-value: 2.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 545521739  580 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSI---KPERVCNPCHEHLMK 631
Cdd:pfam01363  12 CMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTLQK 68
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
580-625 2.23e-08

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


Pssm-ID: 277269 [Multi-domain]  Cd Length: 63  Bit Score: 50.86  E-value: 2.23e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 545521739 580 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPC 625
Cdd:cd15730   12 CMACGKGFSVTvrKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDAC 59
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
286-559 2.46e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.42  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  286 EELNRHLNATVNNL---QAKVDALEKSNTKLTEELAVANnRIITLQEEMERvKEESSYILESNRKGPKQDRTSEgqALSE 362
Cdd:COG1196   175 EEAERKLERTEENLerlEDLLEELEKQLEKLERQAEKAE-RYQELKAELRE-LELALLLAKLKELRKELEELEE--ELSR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  363 ARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-- 440
Cdd:COG1196   251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELke 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  441 --SELNSRLEEKTNQM---AATIKQLEQRLRQAE--RGRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRHQLELELKQ 513
Cdd:COG1196   331 kiEALKEELEERETLLeelEQLLAELEEAKEELEekLSALLEELEEL--FEALREELAELEAELAEIRNELEELKREIES 408
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 545521739  514 ERERRLQNNRSIPGKGSQKP--EPKTDGKHKIQEENVKLKKPLDESHR 559
Cdd:COG1196   409 LEERLERLSERLEDLKEELKelEAELEELQTELEELNEELEELEEQLE 456
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
272-524 8.87e-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: 55.45  E-value: 8.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   272 DGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERV---KEESSYILESNRK- 347
Cdd:TIGR02168  266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELAEELAELEEk 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   348 --GPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHE 425
Cdd:TIGR02168  346 leELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   426 LAFKLQSsdlgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFkQDFGDKINSLQLEVEELtrQRH 505
Cdd:TIGR02168  426 LLKKLEE-----AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSL--ERL 497
                          250
                   ....*....|....*....
gi 545521739   506 QLELELKQERERRLQNNRS 524
Cdd:TIGR02168  498 QENLEGFSEGVKALLKNQS 516
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
580-625 1.32e-07

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


Pssm-ID: 277273 [Multi-domain]  Cd Length: 61  Bit Score: 48.48  E-value: 1.32e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 545521739 580 CQLCQEDGS--LTKNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPC 625
Cdd:cd15734   11 CSVCKRPFSprLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
327-585 1.40e-07

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: 54.69  E-value: 1.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   327 LQEEMERVKEESsYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQ 406
Cdd:TIGR02169  672 EPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   407 DALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ 467
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   468 AERGRQSAELDNRLFK---QDFGDKINSLQLEVEELTRQ--RHQLEL--------ELKQERERRLQNNRSIPGKGSQKPE 534
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEEleELEAALrdlesrlgDLKKERDELEAQLRELERKIEELEA 910
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 545521739   535 PKTDGKHKIQEENVKLKKPLDESHRLpsRPVDGQDQPPPSEKPQICQLCQE 585
Cdd:TIGR02169  911 QIEKKRKRLSELKAKLEALEEELSEI--EDPKGEDEEIPEEELSLEDVQAE 959
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
580-625 2.14e-07

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


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 47.97  E-value: 2.14e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 545521739 580 CQLCQED--GSLTKNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPC 625
Cdd:cd15732   11 CYGCEREfwLASRKHHCRNCGNVFCGSCCNQKLPVPSQqlFEPSRVCKSC 60
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
570-625 3.14e-07

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


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 47.72  E-value: 3.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545521739 570 QPP---PSEKPQICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSI--KPERVCNPC 625
Cdd:cd15731    1 DPPlwvPDEACPQCMACSAPFTVLrrRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
269-518 6.38e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 6.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   269 SEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnRKG 348
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   349 PKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 428
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   429 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRqaERGRQSAELDNRLfKQDFGDKINSLQLEVEELTRQRHQL- 507
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-ENKIEDDEEEARRRLKRLENKIKELg 985
                          250
                   ....*....|....*..
gi 545521739   508 ------ELELKQERERR 518
Cdd:TIGR02168  986 pvnlaaIEEYEELKERY 1002
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
269-517 9.15e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.02  E-value: 9.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  269 SEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKg 348
Cdd:COG1196   747 EELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERE----LESLEQ- 821
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  349 PKQDRTSEGQALSEARKHLKEE-TQLRLD---VEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKH 424
Cdd:COG1196   822 RRERLEQEIEELEEEIEELEEKlDELEEEleeLEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELA 901
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  425 ELAFKLQS-----SDLGVKQK---SELNSRLEEKTNQMAATI-KQLEQRLRQAERGRQSAELDNRLFKQDFgdkiNSLQL 495
Cdd:COG1196   902 ELKEEIEKlrerlEELEAKLErleVELPELEEELEEEYEDTLeTELEREIERLEEEIEALGPVNLRAIEEY----EEVEE 977
                         250       260
                  ....*....|....*....|..
gi 545521739  496 EVEELTRQRHQLELELKQERER 517
Cdd:COG1196   978 RYEELKSQREDLEEAKEKLLEV 999
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
277-578 1.22e-06

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: 51.45  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 277 AILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyilESNRKGPkqdrtse 356
Cdd:NF033930 105 AYVKYRKAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAEFNKVRAKVVPEAEELAETKKKAE---EAKAEEP------- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 357 gqalsEARKHLKEETQLRLDVEKELEiqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG 436
Cdd:NF033930 175 -----VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 437 --VKQ--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RGRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQLELEL 511
Cdd:NF033930 239 dyIKEglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSD 318
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545521739 512 KQERERRLQnnrsipgkGSQKpePKTDGKHKIQEENVKLKKPLDEshrlPSRPVDGQDQPPPSEKPQ 578
Cdd:NF033930 319 NNVADYYKE--------ALEK--DLATKKAELEKTQKDLDKALNE----LGPDGDEEETPAPAPQPE 371
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
580-629 2.03e-06

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


Pssm-ID: 277260 [Multi-domain]  Cd Length: 61  Bit Score: 45.46  E-value: 2.03e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 545521739 580 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPS-SI-KPERVCNPCHEHL 629
Cdd:cd15720    8 CHRCRVQFGVFqrKHHCRACGQVFCGKCSSKSSTIPKfGIeKEVRVCDPCYEKL 61
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
580-629 2.28e-06

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


Pssm-ID: 277259 [Multi-domain]  Cd Length: 65  Bit Score: 45.07  E-value: 2.28e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 545521739 580 CQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPS--SIKPERVCNPCHEHL 629
Cdd:cd15719   12 CTGCSVRFSLTerRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
269-527 2.45e-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: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   269 SEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEElavannRIITLQEEMERVKEESSYILESNRKG 348
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   349 PKQDRTSEGQA----------LSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQ 415
Cdd:TIGR02169  314 ERELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREK 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   416 LDDLR----ALKHELAFKLQSSDLGVKQKSELNS---RLEEKTNQMAATIKQLEQRLRQAERGRQSAELDnrlfKQDFGD 488
Cdd:TIGR02169  394 LEKLKreinELKRELDRLQEELQRLSEELADLNAaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQ 469
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 545521739   489 KINSLQLEVEELTRQRHQLELELKQERERRLQNNRSIPG 527
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
570-625 3.54e-06

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


Pssm-ID: 277266 [Multi-domain]  Cd Length: 64  Bit Score: 44.68  E-value: 3.54e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545521739 570 QPP--PSEKPQICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLP--SSIKPERVCNPC 625
Cdd:cd15727    1 EPPwvPDKECPVCMSCKKKFDFFkrRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
572-626 4.48e-06

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


Pssm-ID: 277257 [Multi-domain]  Cd Length: 61  Bit Score: 44.28  E-value: 4.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545521739 572 PPSEKPqICQLCQEdgslTK-NV------CKNCRGTFCNACSTNELPLPS-SIKPERVCNPCH 626
Cdd:cd15717    4 PDSEAP-VCMHCKK----TKfTAinrrhhCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
PRK11281 PRK11281
mechanosensitive channel MscK;
285-507 5.90e-06

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 49.52  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  285 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVKEESSY----------ILESNRKGPKQDRT 354
Cdd:PRK11281  123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRP 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  355 SE------GQALSEA-----RKHLKEETQL------RLDvEKELEIQismRQEMELA----------MKMLEKDVCEKQD 407
Cdd:PRK11281  192 SQrvllqaEQALLNAqndlqRKSLEGNTQLqdllqkQRD-YLTARIQ---RLEHQLQllqeainskrLTLSEKTVQEAQS 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  408 ALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERG--------RQSAELDN 479
Cdd:PRK11281  268 QDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLSR 340
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 545521739  480 RLFKQ-----------DFGDKINSLQLEVEELTRQRHQL 507
Cdd:PRK11281  341 ILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
292-519 9.17e-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: 9.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  292 LNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDRTSEGQALSEARKHLKEET 371
Cdd:COG1196   300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLE-ELEQLLAELEEAKEELEEKLSALLEELEELF 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  372 QLRLDVEKELEIQISMRQEmelAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKT 451
Cdd:COG1196   379 EALREELAELEAELAEIRN---ELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQL 455
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  452 NQMAATIKQLEQRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEEL--TRQRHQLELELKQERERRL 519
Cdd:COG1196   456 EELRDRLKELERELAELQEELQRLE-----------KELSSLEARLDRLeaEQRASQGVRAVLEALESGL 514
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
274-476 1.66e-05

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 47.71  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 274 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESsyilesnrkgpkQDR 353
Cdd:COG4372   82 QLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQA------------QDL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 354 TSEGQALSEARKHLKEETQLRLDVEKELEIQISM----RQEMELAMKMLE---KDVCEKQDALVSLRQQLDDLRALKHEL 426
Cdd:COG4372  150 QTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQlksqVLDLKLRSAQIEqeaQNLATRANAAQARTEELARRAAAAQQT 229
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 545521739 427 AFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAE 476
Cdd:COG4372  230 AQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLE 279
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
295-520 1.68e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 295 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTSEgqalSEARKHLKEETQLR 374
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 375 L-DVEKELEIQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 453
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545521739 454 MAATIKQLEQRLRQAErgrqsaELDNRLFKQDfgDKINSLQLEVEELTRQRHQLELELKQERERRLQ 520
Cdd:PRK03918 537 LKGEIKSLKKELEKLE------ELKKKLAELE--KKLDELEEELAELLKELEELGFESVEELEERLK 595
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
591-626 1.75e-05

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


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 42.42  E-value: 1.75e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 545521739 591 KNVCKNCRGTFCNACSTNELPLPSS--IKPERVCNPCH 626
Cdd:cd15733   23 KHHCRNCGNVFCADCSNYKLPIPDEqlYDPVRVCNSCY 60
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
267-525 1.78e-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: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 267 KGSEGDGQITAILDQKnyvEELNRHLNATVNNLQAKVDALEKSN-TKLTEELAVANNRIITLQEEMERVKEESSYILESN 345
Cdd:COG0419  186 KIEELEGQLSELLEDI---EDLLEALEEELKELKKLEEIQEEQEeEELEQEIEALEERLAELEEEKERLEELKARLLEIE 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 346 RKGPKQDRTSEgqalSEARKHLKEETQLRLDVE--KELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALK 423
Cdd:COG0419  263 SLELEALKIRE----EELRELERLLEELEEKIErlEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKL 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 424 HELAFKLQS-SDLGVKQKSELNSRLEEKTNQMAATIKQLEQRL-RQAERGRQSAELDNRLfkQDFGDKINSLQLEVEELT 501
Cdd:COG0419  339 EKLESELEElAEEKNELAKLLEERLKELEERLEELEKELEKALeRLKQLEEAIQELKEEL--AELSAALEEIQEELEELE 416
                        250       260
                 ....*....|....*....|....
gi 545521739 502 RQRHQLELELKQERERRLQNNRSI 525
Cdd:COG0419  417 KELEELERELEELEEEIKKLEEQI 440
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
282-470 2.34e-05

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 47.33  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 282 KNYVEElNRHLNATVNNLQAKVDALEKSNTKLteelavaNNRIITLQEEMERVKEESSYIleSNRKGPKQDRTSEGQALS 361
Cdd:COG4372  154 KTLAEQ-RRQLEAQAQSLQASQKQLQASATQL-------KSQVLDLKLRSAQIEQEAQNL--ATRANAAQARTEELARRA 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 362 EARKHLKEETQLRLDVEKELEIQISMRQEmelamkmlekDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS-DLGVKQK 440
Cdd:COG4372  224 AAAQQTAQAIQQRDAQISQKAQQIAARAE----------QIRERERQLQRLETAQARLEQEVAQLEAYYQAYvRLRQQAA 293
                        170       180       190
                 ....*....|....*....|....*....|....
gi 545521739 441 SELNSRLE----EKTNQMAATIKQLEQRLRQAER 470
Cdd:COG4372  294 ATQRGQVLagaaQRVAQAQAQAQAQAQLLSSANR 327
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
580-626 3.38e-05

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


Pssm-ID: 277299 [Multi-domain]  Cd Length: 59  Bit Score: 41.90  E-value: 3.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 545521739 580 CQLCQEDGSLTK--NVCKNCRGTFCNACSTNELPLPSSI---KPERVCNPCH 626
Cdd:cd15760    8 CDVCRKKFGLFKrrHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
580-626 6.40e-05

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


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 40.57  E-value: 6.40e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 545521739 580 CQLCQEDGSLTKNV--CKNCRGTFCNACSTNELPLPS-SIKPERVCNPCH 626
Cdd:cd15749    2 CFGCAAKFSLFKKEcgCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
328-560 8.49e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  328 QEEMERVKEESSYILESNRKGPKQDRTSEGQALSEARKHLKEEtQLRLDVEKELE-IQIS--------MRQEmELAMKM- 397
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE-RMAMERERELErIRQEerkrelerIRQE-EIAMEIs 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  398 ----LEKDVCEKQDALVSLRQQLDDLRALK-----HELAFKLQSSDLGVKQKSELNSR------LEEKTNQMAATIKQLE 462
Cdd:pfam17380 376 rmreLERLQMERQQKNERVRQELEAARKVKileeeRQRKIQQQKVEMEQIRAEQEEARqrevrrLEEERAREMERVRLEE 455
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  463 Q-RLRQAERGRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRHQLELELKQERERRLQNNRSIPGKGSQKPEPKT--DG 539
Cdd:pfam17380 456 QeRQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEE 533
                         250       260
                  ....*....|....*....|.
gi 545521739  540 KHKIQEENVKLKKPLDESHRL 560
Cdd:pfam17380 534 RRREAEEERRKQQEMEERRRI 554
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
278-510 8.92e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 8.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   278 ILDQK--NYVEELnRHLNATVNNLQAKVDALEKSNTKLTEELAvaNNRIITLQEEMERVKEESSYILESNR--KGPKQDR 353
Cdd:TIGR02169  748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLReiEQKLNRL 824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   354 TSEGQALSEARKHLKEETqlrldveKELEIQISM-RQEMELAMKMLEK---DVCEKQDALVSLRQQLDDLRALKHELAFK 429
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQR-------IDLKEQIKSiEKEIENLNGKKEEleeELEELEAALRDLESRLGDLKKERDELEAQ 897
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   430 LQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAErgrqsaeldnRLFKQDFGDKINSLQLEVEELTRQRHQLEL 509
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE----------DPKGEDEEIPEEELSLEDVQAELQRVEEEI 967

                   .
gi 545521739   510 E 510
Cdd:TIGR02169  968 R 968
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
579-625 1.32e-04

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


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 39.79  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 545521739 579 ICQLCQEDGSLT--KNVCKNCRGTFCNACSTNELPLPSSIKP--ERVCNPC 625
Cdd:cd15745    1 ACAICAKAFSLFrrKYVCRLCGGVVCHSCSSEDLVLSVPDTCiyLRVCKTC 51
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
260-519 1.59e-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: 44.73  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  260 LKDGNSSKGSEGDGQITAILDQKNYVEELNRHLNATvnNLQAKVDALEKSNTkltEELAVANNRIITL-------QEEME 332
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQ---EEIAMEISRMRELerlqmerQQKNE 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  333 RVKEE-----SSYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMElamkmlekdvceKQD 407
Cdd:pfam17380 393 RVRQEleaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE------------RQQ 460
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  408 ALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-----SELNSR----LEEKtNQMAATIKQLEQRLRQ--AERGRQSAE 476
Cdd:pfam17380 461 QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkileKELEERkqamIEEE-RKRKLLEKEMEERQKAiyEEERRREAE 539
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 545521739  477 LDNRlfKQDFGDKINSLQLEVEELTRQRHQLElelKQERERRL 519
Cdd:pfam17380 540 EERR--KQQEMEERRRIQEQMRKATEERSRLE---AMEREREM 577
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
276-449 2.35e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.32  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  276 TAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDRTS 355
Cdd:COG1196   351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLE-RLSERLEDLKEELKE 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  356 EGQALSEARKHLKEetqlrldVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 435
Cdd:COG1196   430 LEAELEELQTELEE-------LNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
                         170
                  ....*....|....
gi 545521739  436 GVKQKSELNSRLEE 449
Cdd:COG1196   503 VRAVLEALESGLPG 516
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
277-517 2.36e-04

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 44.37  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 277 AILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILES-NRKGPKQDRTS 355
Cdd:COG0419  484 EELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKlQLQQLKEELRQ 563
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 356 EGQALSEARKHLKEETQLRLDVEKELEIQISMRQ----EMELAMKMLEK----DVCEKQDALVSLRQQLDDLRALKHELA 427
Cdd:COG0419  564 LEDRLQELKELLEELRLLRTRKEELEELRERLKElkkkLKELEERLSQLeellQSLELSEAENELEEAEEELESELEKLN 643
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 428 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFK-----QDFGDKINSLQLEVEELTR 502
Cdd:COG0419  644 LQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQlreelEELLKKLGEIEQLIEELES 723
                        250
                 ....*....|....*
gi 545521739 503 QRHQLElELKQERER 517
Cdd:COG0419  724 RKAELE-ELKKELEK 737
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
330-469 2.50e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  330 EMERVKEES---SYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQ 406
Cdd:pfam17380 447 EMERVRLEEqerQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545521739  407 DALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQKSELNSRLE--EKTNQMAATIKQLEQRLRQAE 469
Cdd:pfam17380 527 KAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKATEERSRLEamEREREMMRQIVESEKARAEYE 592
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
285-464 3.27e-04

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


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 43.52  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 285 VEELNRHLNATVNNL--------QAKVDALEKSNTkLTEELAVANNRIITLQEEMERVKEesSYILESNRKGpKQDRTSe 356
Cdd:COG4477  279 AEEELGLIQEKIESLydllerevEAKNVVEENLPI-LPDYLEKAKENNEHLKEEIERVKE--SYRLAETELG-SVRKFE- 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 357 gqalsearKHLKEETQLRLDVEKELEIQ-------ISMRQEMELAMKMLEKDVCEKQDALVSLR-------QQLDDLRAL 422
Cdd:COG4477  354 --------KELKELESVLDEILENIEAQevayselQDNLEEIEKALTDIEDEQEKVQEHLTSLRkdelearENLERLKSK 425
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 545521739 423 KHELAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 464
Cdd:COG4477  426 LHEIKRYMEKSNLpGLPE--TFLSLFFTAGHEIQDLMKELSEV 466
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
286-516 3.40e-04

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


Pssm-ID: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   286 EELNRHLNATVNNLQAKVDALEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYILESNRKGPKQDRTSEgQALS 361
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLEEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   362 EARKHLKEE-------TQLRL-------DVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 427
Cdd:pfam01576  163 EFTSNLAEEeekvkslNKLKNkheamisDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAKKE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   428 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVEE-LTRQRHQ 506
Cdd:pfam01576  243 EELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRR----DLGEELEALKTELEDtLDSTAAQ 318
                          250
                   ....*....|
gi 545521739   507 LELELKQERE 516
Cdd:pfam01576  319 QELRSKREQE 328
mukB PRK04863
chromosome partition protein MukB;
360-526 4.55e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  360 LSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 437
Cdd:PRK04863  444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  438 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAErGRQSAELDNRLFKQDF----GDKINSLQLEVEELTRQRHQLELELK 512
Cdd:PRK04863  519 RMRlSELEQRLRQQ--------QRAERLLAEFC-KRLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589
                         170
                  ....*....|....
gi 545521739  513 QERERRLQNNRSIP 526
Cdd:PRK04863  590 QLQARIQRLAARAP 603
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
345-545 6.52e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.78  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  345 NRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEkqdalvsLRQQLDDLRALKH 424
Cdd:COG1196   647 EPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEE-------LRRQLEELERQLE 719
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  425 ELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEELTRQR 504
Cdd:COG1196   720 ELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLE-----------EALAKLKEEIEELEEKR 788
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 545521739  505 HQLELELKQERERRLQNNRSIPGKGSQKPEPKTDGKHKIQE 545
Cdd:COG1196   789 QALQEELEELEEELEEAERRLDALERELESLEQRRERLEQE 829
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
274-524 8.50e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.39  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  274 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilESNRKgpkqdr 353
Cdd:COG1196   268 EIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEK-----IEALK------ 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  354 tsegQALSEARKHLKEETQLRLDVEKELEiqiSMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 433
Cdd:COG1196   337 ----EELEERETLLEELEQLLAELEEAKE---ELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESL 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  434 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEELTRQRHQLELELkQ 513
Cdd:COG1196   410 EERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELE-----------EQLEELRDRLKELERELAELQEEL-Q 477
                         250
                  ....*....|.
gi 545521739  514 ERERRLQNNRS 524
Cdd:COG1196   478 RLEKELSSLEA 488
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
286-556 8.92e-04

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: 42.31  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  286 EELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI--------LESNRKGPKQDRTSEG 357
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkkqlsekqKELEQNNKKIKELEKQ 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  358 -------------QALSEARKHLKEETQLRLDVEKELEIQISMRQ----EMELAMKMLEKDVCEKQDALVSLRQQL---- 416
Cdd:TIGR04523 290 lnqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  417 DDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMaatiKQLEQRLRQAERGRQSAELDNRLFKQ----------DF 486
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKEtiiknnseikDL 445
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  487 GDKINSLQLEVEELTRQRHQLELELKqERERRLQNNRSIPGKGSQKPEPKTDGKHKIQEENVKLKKPLDE 556
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLK-VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
274-546 1.16e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   274 QITAILDQknyvEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILesnrkgpkQDR 353
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA--------QCE 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   354 TSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEME---LAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL 430
Cdd:TIGR00618  455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   431 QSSDLGVKQKSELNSRLEEKTNQmAATIKQLEQRLRQAErgRQSAELDNRLfkqdfGDKINSLQLEVEELtrqRHQLELE 510
Cdd:TIGR00618  535 QTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSF--SILTQCDNRS-----KEDIPNLQNITVRL---QDLTEKL 603
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 545521739   511 LKQERERRLQNNRSIpgkgsQKPEPKTDGKHKIQEE 546
Cdd:TIGR00618  604 SEAEDMLACEQHALL-----RKLQPEQDLQDVRLHL 634
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
591-631 1.23e-03

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


Pssm-ID: 277278 [Multi-domain]  Cd Length: 73  Bit Score: 37.71  E-value: 1.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 545521739 591 KNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPCHEHLMK 631
Cdd:cd15739   26 KHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
286-499 1.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 286 EELNRHLNATVNNLQAKVDALEKSntklTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTSEGQALSEARK 365
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP 599
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 366 HLKEETQLRlDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKlQSSDLGVKQKSELNS 445
Cdd:PRK03918 600 FYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE-ELREEYLELSRELAG 677
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545521739 446 ------RLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRL--FKQDFGDKINSLQLEVEE 499
Cdd:PRK03918 678 lraeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAleRVEELREKVKKYKALLKE 739
COG5281 COG5281
Phage-related minor tail protein [Mobilome: prophages, transposons];
252-564 1.61e-03

Phage-related minor tail protein [Mobilome: prophages, transposons];


Pssm-ID: 227606 [Multi-domain]  Cd Length: 833  Bit Score: 41.55  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 252 GVIDFSMYLKDGNSSKGSEGDGQITAILDQKNYVEELNRHLnATVNNLQAKVDALEKSNTKLTEELavaNNRIITLQEEM 331
Cdd:COG5281  311 AMDDRTARVKENMGTLETAWDALADAAKKMWDAVLGIGRED-KQAALLAAKLAAEKLARVTAQGAL---NARLKLAQDDL 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 332 ERVKEE-SSYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVcEKQDALV 410
Cdd:COG5281  387 TQAELNyAAADQAANQEGALNAREDEAEVLSTQEERRDILKNLLADAEKRTARQEELNKALAKAKILQADKA-AKAYQED 465
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 411 SLRQQLDDLR--------------ALKHELAFKLQSSDL-GVKQKSELNSRLEEKTNQMAATIKqLEQRLRQAERgrQSA 475
Cdd:COG5281  466 ILQREAQSRGktaaaersqeqmtaALKALLAFQQQIADLsGAKEKASDQKSLLWKAEEQYALLK-EEAKQRQLQE--QKA 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 476 ELDnrlfkqdfgdkinsLQLEVEELTRqrhQLELELKQERERRLQnnrSIPGKGSQKPEPKTDGKHKIQEENVKLKKPLD 555
Cdd:COG5281  543 LLE--------------HKKETLEYTS---QLAELLDQQADRFEL---SAQAAGSQKERGSDLYREALAQNAAALNKALN 602

                 ....*....
gi 545521739 556 ESHRLPSRP 564
Cdd:COG5281  603 ELAAYWSAL 611
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
286-519 1.62e-03

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: 41.64  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   286 EELNRHLNATVNNLQA----KVDALEKSNTKLtEELavannRIITLQEEmeRVKEESSYIL-----ESNRKGPKQDRTSE 356
Cdd:pfam15921  141 EDLRNQLQNTVHELEAakclKEDMLEDSNTQI-EQL-----RKMMLSHE--GVLQEIRSILvdfeeASGKKIYEHDSMST 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   357 ------GQALSEARKHLKEETQLR----LDVEKELEIQISMRQ-EMELAMKM----LEKDVCEKQDALVSLRQQLDDLRA 421
Cdd:pfam15921  213 mhfrslGSAISKILRELDTEISYLkgriFPVEDQLEALKSESQnKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARS 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   422 LKHELAFKL----------------QSSDLGvKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQD 485
Cdd:pfam15921  293 QANSIQSQLeiiqeqarnqnsmymrQLSDLE-STVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQE 371
                          250       260       270
                   ....*....|....*....|....*....|....
gi 545521739   486 FGDKINSLQLEVEELtrQRHQLELELKQERERRL 519
Cdd:pfam15921  372 SGNLDDQLQKLLADL--HKREKELSLEKEQNKRL 403
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
292-550 2.51e-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: 40.77  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  292 LNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEES----SYILESNRKGPKQDRTSegQALSEARKHL 367
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIknleSQINDLESKIQNQEKLN--QQKDEQIKKL 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  368 KEETQLrldVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSL-------RQQLDDL----RALKHELAFKLQSSDLG 436
Cdd:TIGR04523 418 QQEKEL---LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLsrsiNKIKQNLEQKQKELKSK 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  437 VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ-----AERGRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRHQle 508
Cdd:TIGR04523 495 EKELKKLNeekKELEEKVKDLTKKISSLKEKIEKlesekKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE-- 572
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 545521739  509 leLKQERERRLQNNRSIPGKGSQKPEPKTDGKHKIQEENVKL 550
Cdd:TIGR04523 573 --LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
580-625 2.91e-03

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


Pssm-ID: 277265  Cd Length: 58  Bit Score: 36.38  E-value: 2.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 545521739 580 CQLCQEDGS--LTKNVCKNCRGTFCNACSTNELPLPSSIKPERVCNPC 625
Cdd:cd15726   10 CLDCKSEFSwmVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
311-520 2.94e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   311 TKLTEELAVANNRIITLQEEMERVKEessyILESNRKgpkQDRTSEGQA-LSEARKHLKEE-TQLRLDVE-KELEIQISM 387
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLED----ILNELER---QLKSLERQAeKAERYKELKAElRELELALLvLRLEELREE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739   388 RQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS--SDLG--VKQKSELNSRLEEKTNQMAATIKQLEQ 463
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqKELYalANEISRLEQQKQILRERLANLERQLEE 320
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 545521739   464 RLRQAERGRQSAELDNRLFKQdFGDKINSLQLEVEELtRQRHQLELELKQERERRLQ 520
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAE-LEEKLEELKEELESL-EAELEELEAELEELESRLE 375
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
288-468 2.95e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.81  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  288 LNRHLNATVNNLQAKVDALEK--SNTKLTEELAVANNRII----TLQEEMERVKEessyILESNRKGPKQdRTSEGQALS 361
Cdd:PRK10929   80 LSAELRQQLNNERDEPRSVPPnmSTDALEQEILQVSSQLLeksrQAQQEQDRARE----ISDSLSQLPQQ-QTEARRQLN 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739  362 EARKHLK-------------------EETQLRLDVEkELEI-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDD 418
Cdd:PRK10929  155 EIERRLQtlgtpntplaqaqltalqaESAALKALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNS 233
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 545521739  419 LRALKHELAFKL------QSSDL--GVKQKSELNSRLEEKTNQMAATIKQLEQRLRQA 468
Cdd:PRK10929  234 QRQREAERALEStellaeQSGDLpkSIVAQFKINRELSQALNQQAQRMDLIASQQRQA 291
M_group_A_cterm NF033777
M protein C-terminal domain; M protein (emm) is an important virulence protein and ...
336-474 3.04e-03

M protein C-terminal domain; M protein (emm) is an important virulence protein and serology-defining surface antigen of Streptococcus pyogenes (group A Streptococcus). M protein has an amino-terminal YSIRK-type signal sequence (associated with cross-wall targeting in dividing cells), and a C-terminal LPXTG domain for processing by sortase and covalent attachment to the Gram-positive cell wall. Past the signal peptide, M protein has a hypervariable region, but this HMM describes only the well-conserved region C-terminal to the hypervariable region. It discriminates M protein from two related proteins, Enn and Mrp.


Pssm-ID: 411361 [Multi-domain]  Cd Length: 218  Bit Score: 39.43  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 336 EESSYILESNRKGPKQDRTSEGQALSEARKHLKEETQLRLDVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ 415
Cdd:NF033777   8 EEQNKISEASRKGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSK 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545521739 416 LDDLRALKHELAfklQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQS 474
Cdd:NF033777  88 LAALEKLNKELE---ESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAGKAS 143
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
567-629 3.20e-03

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


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 36.56  E-value: 3.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545521739 567 GQDQP---PPSEKPQiCQLCQEDGSLTK--NVCKNCRGTFCNACSTNELPLPS-SIKPERVCNPCHEHL 629
Cdd:cd15729    1 GKVAPvwvPDSEAPN-CMQCEVKFTFTKrrHHCRACGKVLCSACCSLKARLEYlDNKEARVCVPCYQTL 68
xseA PRK00286
exodeoxyribonuclease VII large subunit; Reviewed
394-524 5.80e-03

exodeoxyribonuclease VII large subunit; Reviewed


Pssm-ID: 234714  Cd Length: 438  Bit Score: 39.41  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 394 AMKMLEKDVCEKQDALVSLRQQLddLRALKHELAFKLQSSDLgvkqkseLNSRL-----EEKTNQMAATIKQLEQRLRQA 468
Cdd:PRK00286 254 AAELAVPDRAELLQRLQQLQQRL--ARAMRRRLEQKRQRLDQ-------LARRLkfqspERLLAQQQQRLDRLQQRLQRA 324
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545521739 469 ------ERGRQSAELDNRLFKQDFGDKINSLQLEVEEL-TRQRHQLELELKQERERrLQNNRS 524
Cdd:PRK00286 325 lerrlrLAKQRLERLSQRLQQQNPQRRIERAQQRLEQLeQRLRRAMRRQLKRKRQR-LEALAQ 386
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
285-464 6.18e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.43  E-value: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 285 VEELNRHLNATVNNL----QAKVDA---LEKSNTKLTEELAVANNRIITLQEEMERVKEesSYILesnrkgpkqdrtSEG 357
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREVKArkyVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTL------------NES 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 358 QaLSEARKHLKEETQLR---LDVEKELEIQ-------ISMRQEMELAMKMLEKDVCEKQDALVSL-------RQQLDDLR 420
Cdd:PRK04778 346 E-LESVRQLEKQLESLEkqyDEITERIAEQeiayselQEELEEILKQLEEIEKEQEKLSEMLQGLrkdeleaREKLERYR 424
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 545521739 421 ALKHELAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 464
Cdd:PRK04778 425 NKLHEIKRYLEKSNLpGLPE--DYLEMFFEVSDEIEALAEELEEK 467
CwlO1 COG3883
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
292-468 6.18e-03

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


Pssm-ID: 226400 [Multi-domain]  Cd Length: 265  Bit Score: 38.93  E-value: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 292 LNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEM-ERVK------EESSY---ILESNRKGPKQDRTSEGQALS 361
Cdd:COG3883   64 IQSKIDELQKEIDQSKAEIKKLQKEIAELKENIVERQELLkKRARamqvngTATSYidvILNSKSFSDLISRVTAISVIV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 362 EARKHL---KEETQLRL-----DVEKELEIQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELafklqss 433
Cdd:COG3883  144 DADKKIleqQKEDKKSLeekqaALEDKLETLVALQNELETQLNSLNSQKAEKNALIAALAAKEASALGEKAAL------- 216
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 545521739 434 dlgVKQKS-ELNSRLEEKTNQMAATIKQLEQRLRQA 468
Cdd:COG3883  217 ---EEQKAlAEAAAAEAAKQEAAAKAAAQEQAALQA 249
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
283-477 9.46e-03

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 38.65  E-value: 9.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 283 NYVEELNRHLNATVNNLQAKVDaLEKSNTKLTEELAvANNRIITLQEEMERVKE-ESSYILESNRKGPKQDRTSEGQALS 361
Cdd:COG4487    2 KEIKVPIQTKPFTIPKCEDSIK-GEQARYKQIEQED-QSRILNTLEEFEKEANEkRAQYRSAKKKELSQLEEQLINQKKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 362 EARKHLKEETQLRLDVEKE---LEIQISMRQEMELAMKMLEKDVCEKQDALVSL-----------RQQLDDLRALKHELA 427
Cdd:COG4487   80 QKNLFNEQIKQFELALQDEiakLEALELLNLEKDKELELLEKELDELSKELQKQlqntaeiiekkRENNKNEERLKFENE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 545521739 428 FKLQSSDLGVKQKSElnSRLEEKTNQM--AATIKQLEQRLRQAERGRQSAEL 477
Cdd:COG4487  160 KKLEESLELEREKFE--EQLHEANLDLefKENEEQRESKWAILKKLKRRAEL 209
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
292-472 9.76e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 225288  Cd Length: 652  Bit Score: 38.92  E-value: 9.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 292 LNATVNNLQAKVDALEKSNTKLTEELAVAN-NRI-------ITLQEEMERVKEESSyilesnrkgPKQDRTSEGQALSEA 363
Cdd:COG2433  347 LAAAYKAYLAYKPKLEKVERKLPELGIWKDvERIkalvirgYPLAEALSKVKEEER---------PREKEGTEEEERREI 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545521739 364 RKHLKEETQLRLDVEKeLEIQIsmrqemelamKMLEKDVCEKQDALVSLRQQLDDLRAlkhELAFKLQSsDLGVKQKSEL 443
Cdd:COG2433  418 TVYEKRIKKLEETVER-LEEEN----------SELKRELEELKREIEKLESELERFRR---EVRDKVRK-DREIRARDRR 482
                        170       180
                 ....*....|....*....|....*....
gi 545521739 444 NSRLEEKTNQMAATIKQLEQRLRQAERGR 472
Cdd:COG2433  483 IERLEKELEEKKKRVEELERKLAELRKMR 511
 
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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