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Conserved domains on  [gi|767931421|ref|XP_011530053|]
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protein RUFY3 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
128-283 1.62e-100

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


:

Pssm-ID: 439058  Cd Length: 156  Bit Score: 303.46  E-value: 1.62e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17696   81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
611-645 4.75e-15

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: 69.37  E-value: 4.75e-15
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767931421 611 NVCKNCSGTFCDACSTNELPLPSSI-KLERVCNPCH 645
Cdd:cd15744   17 HNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
332-600 3.43e-11

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 66.66  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  332 RHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEGQA--LSEARKHL 409
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  410 KEETQLRLDVEKELEMQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 488
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  489 LEEKTNQMA---ATIKQLEQRL-----RQAERSRQSAELDNRLFK-----QDFGDKINSLQLEVEELTRQRNQLELEL-- 553
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELae 471
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767931421  554 KQEKERRLQNDRSIPGRGSQKSESKMDGKHKMQEENVKLKKPLEESH 600
Cdd:COG1196   472 LQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVY 518
PHA03247 super family cl33720
large tegument protein UL36; Provisional
5-100 2.08e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421    5 PPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPD-SPVAAPffllYPGDGGAGFGVrPPP 83
Cdd:PHA03247 2829 PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPvRRLARP----AVSRSTESFAL-PPD 2903
                          90
                  ....*....|....*..
gi 767931421   84 QQQRSwRTPPSPGSPLP 100
Cdd:PHA03247 2904 QPERP-PQPQAPPPPQP 2919
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
128-283 1.62e-100

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 303.46  E-value: 1.62e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17696   81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
163-286 1.41e-46

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: 426965  Cd Length: 136  Bit Score: 160.94  E-value: 1.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  163 QFFVVMEHCLKHGLKAKKT-----------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLAL 231
Cdd:pfam02759   1 SLCAALEALLSHGLKRKALsaslsliegyyGLLPERSFWDLLERVGKLVPPAEELLSSVQALEQIHTSDGRGRAWIRLAL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421  232 MQKKLSEYMKALINKKELLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 286
Cdd:pfam02759  81 NEKLLEQWLNLLLSNKELLSKYYEPWALLRDPEFVeILLGLLVGLSALDFNLCLDL 136
RUN smart00593
domain involved in Ras-like GTPase signaling;
223-285 3.75e-19

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 81.51  E-value: 3.75e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767931421   223 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 285
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
611-645 4.75e-15

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: 69.37  E-value: 4.75e-15
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767931421 611 NVCKNCSGTFCDACSTNELPLPSSI-KLERVCNPCH 645
Cdd:cd15744   17 HNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
332-600 3.43e-11

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 66.66  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  332 RHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEGQA--LSEARKHL 409
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  410 KEETQLRLDVEKELEMQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 488
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  489 LEEKTNQMA---ATIKQLEQRL-----RQAERSRQSAELDNRLFK-----QDFGDKINSLQLEVEELTRQRNQLELEL-- 553
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELae 471
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767931421  554 KQEKERRLQNDRSIPGRGSQKSESKMDGKHKMQEENVKLKKPLEESH 600
Cdd:COG1196   472 LQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVY 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-591 2.51e-10

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: 63.92  E-value: 2.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   314 DGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKG 390
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   391 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 470
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   471 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRqsAELDNRLfkQDFGDKINSLQLEVEELTRQRNQLE 550
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEALALLRSELEELS 900
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 767931421   551 LELKQEKERRLQNDRSIPGRGSQKSESKMD-GKHKMQEENVK 591
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRlEGLEVRIDNLQ 942
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
337-598 6.08e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 6.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 337 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEgqalSEARKHLKEETQLR 416
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 417 L-DVEKELEMQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 495
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 496 MAATIKQLEQRLRQAErsrqsaELDNRLFKQDfgDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDRSIpgrgSQKS 575
Cdd:PRK03918 537 LKGEIKSLKKELEKLE------ELKKKLAELE--KKLDELEEELAELLKELEELGFESVEELEERLKELEPF----YNEY 604
                        250       260
                 ....*....|....*....|...
gi 767931421 576 ESKMDGKHKMQEENVKLKKPLEE 598
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEE 627
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
613-648 1.58e-06

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: 45.89  E-value: 1.58e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 767931421   613 CKNCSGTFCDACSTNELPLPSS--IKLERVCNPCHKHL 648
Cdd:smart00064  29 CRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
329-597 2.13e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.88  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  329 ELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTA----EGQALSE 404
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATtcslEELLRTE 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  405 ARKHLKEETQLRL---DVEK---ELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQ---QLDDLRALKHELAFKLQSS 475
Cdd:pfam05483 369 QQRLEKNEDQLKIitmELQKkssELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekIAEELKGKEQELIFLLQAR 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  476 DlgvKQKSELNSrleektnQMAATIKQLEQRLRQAERSRqsAELDNRLFKQ-DFGDKINSLQLEVEELTRQRNQLELELK 554
Cdd:pfam05483 449 E---KEIHDLEI-------QLTAIKTSEEHYLKEVEDLK--TELEKEKLKNiELTAHCDKLLLENKELTQEASDMTLELK 516
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767931421  555 QEKERRLQNdrsipgrgsQKSESKMDGK-HKMQEENVKLKKPLE 597
Cdd:pfam05483 517 KHQEDIINC---------KKQEERMLKQiENLEEKEMNLRDELE 551
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
613-650 6.41e-06

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


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 44.29  E-value: 6.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767931421  613 CKNCSGTFCDACSTNELPLPSSI---KLERVCNPCHKHLMK 650
Cdd:pfam01363  28 CRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTLQK 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
5-100 2.08e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421    5 PPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPD-SPVAAPffllYPGDGGAGFGVrPPP 83
Cdd:PHA03247 2829 PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPvRRLARP----AVSRSTESFAL-PPD 2903
                          90
                  ....*....|....*..
gi 767931421   84 QQQRSwRTPPSPGSPLP 100
Cdd:PHA03247 2904 QPERP-PQPQAPPPPQP 2919
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
128-283 1.62e-100

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 303.46  E-value: 1.62e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17696   81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
128-283 4.58e-97

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


Pssm-ID: 439057  Cd Length: 156  Bit Score: 294.58  E-value: 4.58e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17695    1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17695   81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
128-282 1.50e-95

RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439043  Cd Length: 155  Bit Score: 290.63  E-value: 1.50e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17681    1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767931421 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 282
Cdd:cd17681   81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
128-283 2.98e-92

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


Pssm-ID: 439056  Cd Length: 156  Bit Score: 282.18  E-value: 2.98e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17694    1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17694   81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
163-286 1.41e-46

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: 426965  Cd Length: 136  Bit Score: 160.94  E-value: 1.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  163 QFFVVMEHCLKHGLKAKKT-----------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLAL 231
Cdd:pfam02759   1 SLCAALEALLSHGLKRKALsaslsliegyyGLLPERSFWDLLERVGKLVPPAEELLSSVQALEQIHTSDGRGRAWIRLAL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421  232 MQKKLSEYMKALINKKELLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 286
Cdd:pfam02759  81 NEKLLEQWLNLLLSNKELLSKYYEPWALLRDPEFVeILLGLLVGLSALDFNLCLDL 136
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
131-282 1.42e-36

RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.


Pssm-ID: 439046  Cd Length: 150  Bit Score: 134.06  E-value: 1.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 131 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLG--QNKSFWGPLELVEKLVPEAAeiTA 208
Cdd:cd17684    1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IA 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767931421 209 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 282
Cdd:cd17684   77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
139-282 1.76e-33

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


Pssm-ID: 439038  Cd Length: 154  Bit Score: 125.62  E-value: 1.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 139 SIKGLIESALNLGR-------TLDSDYAPLQQFFVVMEHCLKHGLKAKKtFLGQNKSFWGPLELVEKLVPEAAEITA--S 209
Cdd:cd17671    2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKQAirD 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767931421 210 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANF 282
Cdd:cd17671   81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
131-283 1.91e-26

RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.


Pssm-ID: 439062  Cd Length: 151  Bit Score: 105.44  E-value: 1.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 131 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQN--KSFWGPLELVEKLVPEAAeiTA 208
Cdd:cd17700    1 NLITVCRFSVKTLIDRSCF--ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHNC--IC 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767931421 209 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17700   77 SIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
131-283 7.46e-24

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


Pssm-ID: 439061  Cd Length: 151  Bit Score: 98.17  E-value: 7.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 131 NLMNMAKLSIKGLIESALnlGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQnKSFWGPLELVEKLVPEaaEIT 207
Cdd:cd17699    1 NLITVCRFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVPN--NCI 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17699   76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
RUN smart00593
domain involved in Ras-like GTPase signaling;
223-285 3.75e-19

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 81.51  E-value: 3.75e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767931421   223 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 285
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
140-279 5.39e-17

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


Pssm-ID: 439044  Cd Length: 150  Bit Score: 78.42  E-value: 5.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 140 IKGLIESALNLGRTLDSDYAP-LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLE-LVEKLVPEA---AEITASVKDLP 214
Cdd:cd17682    2 LKGCVLDLKSEFGEITDPDNPyLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421 215 GLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEE-GAIIAGLLVGLNVID 279
Cdd:cd17682   82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEIlSEILLSLLYQLNEIN 147
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
611-645 4.75e-15

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: 69.37  E-value: 4.75e-15
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767931421 611 NVCKNCSGTFCDACSTNELPLPSSI-KLERVCNPCH 645
Cdd:cd15744   17 HNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
129-275 3.26e-14

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.


Pssm-ID: 439041 [Multi-domain]  Cd Length: 171  Bit Score: 71.08  E-value: 3.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 129 RMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAK-----KTFLGQN------KSFWGPLELV- 196
Cdd:cd17679    1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKfiskvSSVFSGDvdklpePNFWPLLLKFs 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 197 EKlvpeaaEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGL 275
Cdd:cd17679   81 HR------DVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGL 154
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
213-278 1.05e-12

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


Pssm-ID: 439051  Cd Length: 166  Bit Score: 66.49  E-value: 1.05e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767931421 213 LPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVI 278
Cdd:cd17689   93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
613-645 5.86e-12

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: 60.86  E-value: 5.86e-12
                         10        20        30
                 ....*....|....*....|....*....|...
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSIKLERVCNPCH 645
Cdd:cd15721   26 CRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
168-278 1.42e-11

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4.


Pssm-ID: 439059  Cd Length: 150  Bit Score: 62.89  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 168 MEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKK 247
Cdd:cd17697   35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767931421 248 ELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVI 278
Cdd:cd17697  115 ELTGEWYYARSpFLSPELRSDILDSLYELNGV 146
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
332-600 3.43e-11

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 66.66  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  332 RHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEGQA--LSEARKHL 409
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  410 KEETQLRLDVEKELEMQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 488
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  489 LEEKTNQMA---ATIKQLEQRL-----RQAERSRQSAELDNRLFK-----QDFGDKINSLQLEVEELTRQRNQLELEL-- 553
Cdd:COG1196   392 LAEIRNELEelkREIESLEERLerlseRLEDLKEELKELEAELEElqtelEELNEELEELEEQLEELRDRLKELERELae 471
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767931421  554 KQEKERRLQNDRSIPGRGSQKSESKMDGKHKMQEENVKLKKPLEESH 600
Cdd:COG1196   472 LQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVY 518
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
318-556 5.12e-11

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 65.89  E-value: 5.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  318 TAILDQKNYVEELNRHLNA---TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI------LESNR 388
Cdd:COG1196   688 EELKSLKNELRSLEDLLEElrrQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEEL 767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  389 KGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 468
Cdd:COG1196   768 ESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  469 AFKLQSSDlgvKQKSELNSRLEEKTNQMA----------ATIKQLEQRLRQAERSRQSAELDNrlfkQDFGDKINSLQLE 538
Cdd:COG1196   848 EEELEELE---KELEELKEELEELEAEKEeledelkeleEEKEELEEELRELESELAELKEEI----EKLRERLEELEAK 920
                         250
                  ....*....|....*...
gi 767931421  539 VEELTRQRNQLELELKQE 556
Cdd:COG1196   921 LERLEVELPELEEELEEE 938
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
139-260 6.19e-11

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


Pssm-ID: 439042  Cd Length: 145  Bit Score: 60.72  E-value: 6.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 139 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKktflgqNKSFWGpleLVEKLVPEAAEItaSVKDLPGLKT 218
Cdd:cd17680   12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRG------NRGYWP---FVKEFTHKETIK--QIENLPNVTT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767931421 219 PVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALM 260
Cdd:cd17680   81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
169-279 1.23e-10

RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. SGSM2, also called RUN and TBC1 domain-containing protein 1 (RUTBC1), is a GTPase-activating protein for Rab32/38, and regulates melanogenic enzyme trafficking in melanocytes. It also acts as a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins. This model contains the RUN domain of SGSM1 and SGSM2.


Pssm-ID: 439049  Cd Length: 161  Bit Score: 60.38  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 169 EHCLKHGLKAKK-TFLGQNKSFwGPLELVEKLVPEAAEITASVKDL------PGLKTPVGRGRA-------------WLR 228
Cdd:cd17687   31 DACLLHGLRKRAlGLFRSSSTF-SLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIR 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767931421 229 LALMQKKLSEYMKALINKKellSEFYEPNALMME-EEGAIIAGLLVGLNVID 279
Cdd:cd17687  110 IALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
328-601 1.67e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 64.35  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  328 EELNRHLNATVNNL---QAKVDALEKSNTKLTEELAVANnRIITLQEEMERvKEESSYILESNRKGPKQDRTAEgqALSE 404
Cdd:COG1196   175 EEAERKLERTEENLerlEDLLEELEKQLEKLERQAEKAE-RYQELKAELRE-LELALLLAKLKELRKELEELEE--ELSR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  405 ARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-- 482
Cdd:COG1196   251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELke 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  483 --SELNSRLEEKTNQM---AATIKQLEQRLRQAE--RSRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRNQLELELKQ 555
Cdd:COG1196   331 kiEALKEELEERETLLeelEQLLAELEEAKEELEekLSALLEELEEL--FEALREELAELEAELAEIRNELEELKREIES 408
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767931421  556 EKERRLQNDRSIPGRGSQKS--ESKMDGKHKMQEENVKLKKPLEESHR 601
Cdd:COG1196   409 LEERLERLSERLEDLKEELKelEAELEELQTELEELNEELEELEEQLE 456
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-591 2.51e-10

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: 63.92  E-value: 2.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   314 DGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKG 390
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   391 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 470
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   471 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRqsAELDNRLfkQDFGDKINSLQLEVEELTRQRNQLE 550
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEALALLRSELEELS 900
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 767931421   551 LELKQEKERRLQNDRSIPGRGSQKSESKMD-GKHKMQEENVK 591
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRlEGLEVRIDNLQ 942
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
134-282 3.63e-10

RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and Phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. This model represents the RUN domain of FYCO1.


Pssm-ID: 439060  Cd Length: 158  Bit Score: 58.94  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 134 NMAKLSIKGLIESALNLGRTLDSDYAP-------LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPL-ELVEKlVPEAAE 205
Cdd:cd17698    2 SQLQKIIRDLQDCVTELKKEFEETGEPitddsttLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFcECLAK-VKGLND 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767931421 206 ITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEP-NALMMEEEGAIIAGLLVGLNviDANF 282
Cdd:cd17698   81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPrSVFLNHKYSSDIINSLYDLN--EVQF 156
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
174-283 8.61e-10

RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the first RUN domain of DENND5.


Pssm-ID: 439039  Cd Length: 183  Bit Score: 58.56  E-value: 8.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 174 HGLKAKktflgQNKS-FWGPL----ELVEKLVPEAAEITA---SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALIN 245
Cdd:cd17677   65 HGLQTK-----QGKSaLWSHLlayqENEERLKPLPESLLFdmkNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767931421 246 KKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 283
Cdd:cd17677  140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVDY-FC 177
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
613-653 1.46e-09

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: 54.69  E-value: 1.46e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSIKLERVCNPCHKHLMKQYS 653
Cdd:cd15758   31 CRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
613-655 1.57e-09

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: 54.65  E-value: 1.57e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSIKLERVCNPCHKHLMKQYSTS 655
Cdd:cd15759   29 CRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
148-281 1.71e-09

RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (RUBCN) and similar proteins; RUBCN, also called rubicon, or beclin-1 associated RUN domain containing protein (Baron), is part of a Beclin-1-Vps34-containing autophagy complex. It negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. It is also an important negative regulator of the innate immune response, enhances viral replication and may play a role in viral immune evasion. This model contains the RUN domain of RUBCN.


Pssm-ID: 439048  Cd Length: 151  Bit Score: 56.89  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 148 LNLGRTLD--SDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNkSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVG-RGR 224
Cdd:cd17686    6 LLLSRSSNvwSTYGGLQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGR 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767931421 225 AWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAiiAGLLVGLNVIDAN 281
Cdd:cd17686   85 LWLRQSLQQHCLSSQLQWLVSDKELLRKYYEDEAFLRQEGYA--TALLICLTAVELN 139
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
316-562 2.31e-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: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  316 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnRKGPKQDR 395
Cdd:COG1196   717 QLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEE--------IEELEEKR 788
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  396 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 475
Cdd:COG1196   789 QALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEEL 868
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  476 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQdfgdKINSLQLEVEELTRQ-RNQLELELK 554
Cdd:COG1196   869 EAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEA----KLERLEVELPELEEElEEEYEDTLE 944

                  ....*...
gi 767931421  555 QEKERRLQ 562
Cdd:COG1196   945 TELEREIE 952
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
311-561 8.31e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.96  E-value: 8.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  311 TEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE-SSYILESNRK 389
Cdd:COG1196   747 EELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERElESLEQRRERL 826
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  390 GPK----QDRTAEGQA-LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMK-------MLEKDVCEKQDALVSLRQQ 457
Cdd:COG1196   827 EQEieelEEEIEELEEkLDELEEELEELEKELEELKEELEELEAEKEELEDELKeleeekeELEEELRELESELAELKEE 906
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  458 LDDLRALKHELAFKLQssdlgvKQKSELNSRLEEKTNQMAATI-KQLEQRLRQAERSRQSAELDNRLFKQDFG---DKIN 533
Cdd:COG1196   907 IEKLRERLEELEAKLE------RLEVELPELEEELEEEYEDTLeTELEREIERLEEEIEALGPVNLRAIEEYEeveERYE 980
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767931421  534 SLQLEVEELTRQRNQLEL---ELKQEKERRL 561
Cdd:COG1196   981 ELKSQREDLEEAKEKLLEvieELDKEKRERF 1011
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
311-560 1.46e-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: 58.14  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   311 TEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnRKG 390
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   391 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 470
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   471 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLrqaeRSRQSAELDNRL-FKQDFGDKINSLQLEVEELTRQRNQL 549
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL----SEEYSLTLEEAEaLENKIEDDEEEARRRLKRLENKIKEL 984
                          250
                   ....*....|....*...
gi 767931421   550 -------ELELKQEKERR 560
Cdd:TIGR02168  985 gpvnlaaIEEYEELKERY 1002
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
369-610 2.45e-08

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: 57.39  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   369 LQEEMERVKEESsYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQ 448
Cdd:TIGR02169  672 EPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   449 DALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ 509
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   510 AERSRQSAELDNRLFK---QDFGDKINSLQLEVEELTRQRNQLELELKQ--------EKER-RLQNDRSIPGRGSQKSES 577
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDlesrlgdlKKERdELEAQLRELERKIEELEA 910
                          250       260       270
                   ....*....|....*....|....*....|....
gi 767931421   578 KMD-GKHKMQEENVKLKKPLEESHRLQPHPMDEQ 610
Cdd:TIGR02169  911 QIEkKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
210-283 2.78e-08

RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B.


Pssm-ID: 439053  Cd Length: 206  Bit Score: 54.68  E-value: 2.78e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767931421 210 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 283
Cdd:cd17691  127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVDY-FC 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
324-589 2.89e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 2.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   324 KNYVEELNRhLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGpKQDRTAEGQALS 403
Cdd:TIGR02168  263 QELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   404 EARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAlkhELafklqssdlgvkqks 483
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN---EI--------------- 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   484 elnSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELdnrlfkQDFGDKINSLQLEVEELTRQRNQLE--LELKQEKERRL 561
Cdd:TIGR02168  403 ---ERLEARLERLEDRRERLQQEIEELLKKLEEAEL------KELQAELEELEEELEELQEELERLEeaLEELREELEEA 473
                          250       260
                   ....*....|....*....|....*...
gi 767931421   562 QNDRSIPGRGSQKSESKMDGKHKMQEEN 589
Cdd:TIGR02168  474 EQALDAAERELAQLQARLDSLERLQENL 501
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
314-562 4.64e-08

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 56.31  E-value: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 314 DGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERvKEESSYILESNRKGPKQ 393
Cdd:COG0419  318 EELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEK-ALERLKQLEEAIQELKE 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 394 DRTAEGQALSEARKHLKEETQLRLDVEKELEmQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD----DLRALKHELA 469
Cdd:COG0419  397 ELAELSAALEEIQEELEELEKELEELERELE-ELEEEIKKLEEQINQLESKELMIAELAGAGEKCPvcgqELPEEHEKEL 475
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 470 FKLQSSDLGVKQKSELNSRLEEKTNQmaaTIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQL 549
Cdd:COG0419  476 LELYELELEELEEELSREKEEAELRE---EIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKL 552
                        250
                 ....*....|...
gi 767931421 550 ELELKQEKERRLQ 562
Cdd:COG0419  553 QLQQLKEELRQLE 565
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
312-567 2.01e-07

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 54.38  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 312 EGDGQITAILDQKnyvEELNRHLNATVNNLQAKVDALEKSN-TKLTEELAVANNRIITLQEEMERVKEESSYILESNRKG 390
Cdd:COG0419  189 ELEGQLSELLEDI---EDLLEALEEELKELKKLEEIQEEQEeEELEQEIEALEERLAELEEEKERLEELKARLLEIESLE 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 391 PKQDRTAEgqalSEARKHLKEETQLRLDVE--KELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 468
Cdd:COG0419  266 LEALKIRE----EELRELERLLEELEEKIErlEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKL 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 469 AFKLQS-SDLGVKQKSELNSRLEEKTNQMAATIKQLEQRL-RQAERSRQSAELDNRLfkQDFGDKINSLQLEVEELTRQR 546
Cdd:COG0419  342 ESELEElAEEKNELAKLLEERLKELEERLEELEKELEKALeRLKQLEEAIQELKEEL--AELSAALEEIQEELEELEKEL 419
                        250       260
                 ....*....|....*....|.
gi 767931421 547 NQLELELKQEKERRLQNDRSI 567
Cdd:COG0419  420 EELERELEELEEEIKKLEEQI 440
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
337-598 6.08e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 6.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 337 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEgqalSEARKHLKEETQLR 416
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 417 L-DVEKELEMQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 495
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 496 MAATIKQLEQRLRQAErsrqsaELDNRLFKQDfgDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDRSIpgrgSQKS 575
Cdd:PRK03918 537 LKGEIKSLKKELEKLE------ELKKKLAELE--KKLDELEEELAELLKELEELGFESVEELEERLKELEPF----YNEY 604
                        250       260
                 ....*....|....*....|...
gi 767931421 576 ESKMDGKHKMQEENVKLKKPLEE 598
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEE 627
PRK11281 PRK11281
mechanosensitive channel MscK;
327-549 6.43e-07

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 52.61  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  327 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVKEESSY----------ILESNRKGPKQDR- 395
Cdd:PRK11281  123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  396 ------TAEgQALSEA-----RKHLKEETQL------RLDVEKE----LEMQISMRQEM--ELAMKMLEKDVCEKQDALV 452
Cdd:PRK11281  192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRDYLTAriqrLEHQLQLLQEAinSKRLTLSEKTVQEAQSQDE 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  453 SLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERS--------RQSAELDNRLF 524
Cdd:PRK11281  271 AARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLSRILY 343
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767931421  525 KQ-----------DFGDKINSLQLEVEELTRQRNQL 549
Cdd:PRK11281  344 QQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
312-574 8.70e-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: 52.38  E-value: 8.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   312 EGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEElavannRIITLQEEMERVKEESSYILESNRKGP 391
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKE 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   392 KQDRTAEGQA----------LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQL 458
Cdd:TIGR02169  315 RELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREKL 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   459 DDLralKHELAFKLQSSDLGVKQKSELNSRL----------EEKTNQMAATIKQLEQRLRQAERSRQSAELDnrlfKQDF 528
Cdd:TIGR02169  395 EKL---KREINELKRELDRLQEELQRLSEELadlnaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKY 467
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 767931421   529 GDKINSLQLEVEELTRQRNQLELELKQ-EKERRLQNDRSIPGRGSQK 574
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQRELAEaEAQARASEERVRGGRAVEE 514
RUN_SGSM1 cd17703
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ...
140-274 1.57e-06

RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. This model contains the RUN domain of SGSM1.


Pssm-ID: 439065  Cd Length: 177  Bit Score: 48.85  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 140 IKGLIESALNLgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKT-FLGQNK----------SFWGPLELVEKL--------- 199
Cdd:cd17703    3 VKQIMEEAVTR-KFVHEDSSHIISFCAAVEACVLHGLKRRAAgFLRSNKiaalfmkvgkSFPPAEELCRKVqeleqllen 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 200 ----VPEAAEITASVKDLPGLkTPVGRGRAWLRLALMQKKLSEYMKALInkkELLSEFYEPNALMMEE-EGAIIAGLLVG 274
Cdd:cd17703   82 krnqMQGLQENVRKMPKLPNL-SPQAIKHLWIRTALFEKVLDKIVHYLV---ENSSKYYEKEALLMDPvDGPILASLLVG 157
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
613-648 1.58e-06

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: 45.89  E-value: 1.58e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 767931421   613 CKNCSGTFCDACSTNELPLPSS--IKLERVCNPCHKHL 648
Cdd:smart00064  29 CRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
329-597 2.13e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.88  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  329 ELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTA----EGQALSE 404
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATtcslEELLRTE 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  405 ARKHLKEETQLRL---DVEK---ELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQ---QLDDLRALKHELAFKLQSS 475
Cdd:pfam05483 369 QQRLEKNEDQLKIitmELQKkssELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekIAEELKGKEQELIFLLQAR 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  476 DlgvKQKSELNSrleektnQMAATIKQLEQRLRQAERSRqsAELDNRLFKQ-DFGDKINSLQLEVEELTRQRNQLELELK 554
Cdd:pfam05483 449 E---KEIHDLEI-------QLTAIKTSEEHYLKEVEDLK--TELEKEKLKNiELTAHCDKLLLENKELTQEASDMTLELK 516
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767931421  555 QEKERRLQNdrsipgrgsQKSESKMDGK-HKMQEENVKLKKPLE 597
Cdd:pfam05483 517 KHQEDIINC---------KKQEERMLKQiENLEEKEMNLRDELE 551
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
328-560 2.40e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.79  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  328 EELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEG-------- 399
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikelekq 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  400 -------------QALSEARKHLKEETQLRLDVEKELEMQISMRQ----EMELAMKMLEKDVCEKQDALVSLRQQL---- 458
Cdd:TIGR04523 290 lnqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  459 DDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMaatiKQLEQRLRQAERSRQSAELDNRLFKQDfgdkINSLQLE 538
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKET----IIKNNSE 441
                         250       260
                  ....*....|....*....|..
gi 767931421  539 VEELTRQRNQLELELKQEKERR 560
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTR 463
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
613-645 3.49e-06

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: 44.45  E-value: 3.49e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767931421 613 CKNCSGTFCDACSTNELPLPS--SIKLERVCNPCH 645
Cdd:cd00065   18 CRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
370-603 6.01e-06

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: 49.35  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  370 QEEMERVKEESSYILESNRKgPKQDRTAEGQALSEARKHLKEETQLRLDVEKELE--MQISMRQEME------LAMKM-- 439
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERERELEriRQEERKRELErirqeeIAMEIsr 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  440 ---LEKDVCEKQDALVSLRQQLDDLRALK-----HELAFKLQSSDLGVKQKSELNSR------LEEKTNQMAATIKQLEQ 505
Cdd:pfam17380 377 mreLERLQMERQQKNERVRQELEAARKVKileeeRQRKIQQQKVEMEQIRAEQEEARqrevrrLEEERAREMERVRLEEQ 456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  506 -RLRQAERSRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDRSIPGRGSQKSESKM--DGK 582
Cdd:pfam17380 457 eRQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEER 534
                         250       260
                  ....*....|....*....|.
gi 767931421  583 HKMQEENVKLKKPLEESHRLQ 603
Cdd:pfam17380 535 RREAEEERRKQQEMEERRRIQ 555
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
613-650 6.41e-06

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


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 44.29  E-value: 6.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767931421  613 CKNCSGTFCDACSTNELPLPSSI---KLERVCNPCHKHLMK 650
Cdd:pfam01363  28 CRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTLQK 68
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
334-598 6.48e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.25  E-value: 6.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  334 LNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEES----SYILESNRKGPKQDRTAegQALSEARKHL 409
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIknleSQINDLESKIQNQEKLN--QQKDEQIKKL 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  410 KEETQLrldVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSL-------RQQLDDL----RALKHELAFKLQSSDLG 478
Cdd:TIGR04523 418 QQEKEL---LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLsrsiNKIKQNLEQKQKELKSK 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  479 VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ-----AERSRQSAELDNRLFKQDFGDKINSLQLEVEELtrqrNQLE 550
Cdd:TIGR04523 495 EKELKKLNeekKELEEKVKDLTKKISSLKEKIEKlesekKEKESKISDLEDELNKDDFELKKENLEKEIDEK----NKEI 570
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767931421  551 LELKQEKERRLQNDRSIPGRGSQKSESKMDGKhKMQEENVKLKKPLEE 598
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKEKEKKDLI-KEIEEKEKKISSLEK 617
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
410-598 6.58e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 6.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   410 KEETQLRL-----------DVEKELEMQI-SMRQEMELAMKMLEKDVCEKQdalVSLRQQLDDLRALKHELAFKLQssdl 477
Cdd:TIGR02168  174 RKETERKLertrenldrleDILNELERQLkSLERQAEKAERYKELKAELRE---LELALLVLRLEELREELEELQE---- 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   478 gvkQKSELNSRLEEKTNQMAATIKQLEQ-RLRQAERSRQSAELDNRLFkqdfgdkinSLQLEVEELTRQrnqleLELKQE 556
Cdd:TIGR02168  247 ---ELKEAEEELEELTAELQELEEKLEElRLEVSELEEEIEELQKELY---------ALANEISRLEQQ-----KQILRE 309
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 767931421   557 KERRLQNDRSIPGRGSQKSESKMDgkhKMQEENVKLKKPLEE 598
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLD---ELAEELAELEEKLEE 348
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
328-558 6.62e-06

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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 49.39  E-value: 6.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   328 EELNRHLNATVNNLQAKVDALEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYILESNRKGPKQDRTAEgQALS 403
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLEEEEA-ARQKLqlekVTTEAKIKKMEEDILLLEDQNNKLQKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   404 EARKHLKEE-------TQLRL-------DVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAL----K 465
Cdd:pfam01576  163 EFTSNLAEEeekskslNKLKNkheamisDLEDRLKKEEKGRQELEKAKRKLEGESSDLQEQIAELQAQIAELRAQlakkE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   466 HELAFKLQSSDLGVKQKSELNSRLEEKTNQMAatikQLEQRLRQAERSRQSAELDNRlfkqDFGDKINSLQLEVEE-LTR 544
Cdd:pfam01576  243 EELQAALARLEEETAQKNAALKKLRELEAQLS----ELQEDLESERAARAKAEKQRR----DLGEELEALKTELEDtLDT 314
                          250
                   ....*....|....
gi 767931421   545 QRNQLELELKQEKE 558
Cdd:pfam01576  315 TAAQQELRSKREQE 328
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
613-645 7.44e-06

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: 43.67  E-value: 7.44e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767931421 613 CKNCSGTFCDACSTNELPLP--SSIKLERVCNPCH 645
Cdd:cd15735   25 CRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
302-560 8.84e-06

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: 48.97  E-value: 8.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  302 LKDGNSSKGTEGDGQITAILDQKNYVEELNRHLNATvnNLQAKVDALEKSNTkltEELAVANNRIITL-------QEEME 374
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQ---EEIAMEISRMRELerlqmerQQKNE 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  375 RVKEE-----SSYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKM--LEKDVCEK 447
Cdd:pfam17380 393 RVRQEleaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVerLRQQEEER 472
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  448 QDALVSLRQQLDDlRALKHELAFKLQSSDLGVKQKS---ELNSR--LEEKTNQMAATIKQLEQRLRQAERSRQSAELDNR 522
Cdd:pfam17380 473 KRKKLELEKEKRD-RKRAEEQRRKILEKELEERKQAmieEERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEER 551
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767931421  523 LFKQDFGDKINSLQLEVEELTRQRNQLELELKQEKERR 560
Cdd:pfam17380 552 RRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
PHA03247 PHA03247
large tegument protein UL36; Provisional
5-100 2.08e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421    5 PPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPD-SPVAAPffllYPGDGGAGFGVrPPP 83
Cdd:PHA03247 2829 PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPvRRLARP----AVSRSTESFAL-PPD 2903
                          90
                  ....*....|....*..
gi 767931421   84 QQQRSwRTPPSPGSPLP 100
Cdd:PHA03247 2904 QPERP-PQPQAPPPPQP 2919
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
337-552 2.36e-05

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


Pssm-ID: 430825 [Multi-domain]  Cd Length: 305  Bit Score: 46.66  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  337 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRkgpkqdrtaegQALSEARKHLKEETQLR 416
Cdd:pfam09787  41 GSTALSLELDELRQERDLLREELQQLNQQIEQLRTELQELEAQQQEEAESSR-----------EQLQDLEEQLATERQAR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  417 LDVEKELEmqismRQEMELamKMLEKDVCEKQDALVS-LRQQLDDLRALKHELAFKLQSSdlgvKQKSELNSRLEEKTNQ 495
Cdd:pfam09787 110 REAEAELE-----RLQEEL--RYLEEELRRTKATLQSrIKDREAEIEKLRNQLTNKSQSS----SSQSELENRLHQLTES 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767931421  496 MAATIKQLEQrlRQAERsrqsaeldnrlfkqdfgdkiNSLQLEVEELTRQRNQLELE 552
Cdd:pfam09787 179 LIQKQTMLEA--LSTEK--------------------NSLVLQLERLEQQIKELQGE 213
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
318-491 2.54e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.40  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  318 TAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDRTA 397
Cdd:COG1196   351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLE-RLSERLEDLKEELKE 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  398 EGQALSEARKHLKEETQLRLDVEKELEMQISMRQEmelamkmLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 477
Cdd:COG1196   430 LEAELEELQTELEELNEELEELEEQLEELRDRLKE-------LERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
                         170
                  ....*....|....
gi 767931421  478 GVKQKSELNSRLEE 491
Cdd:COG1196   503 VRAVLEALESGLPG 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
320-552 2.75e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   320 ILDQK--NYVEELnRHLNATVNNLQAKVDALEKSNTKLTEELAvaNNRIITLQEEMERVKEESSYILESNR--KGPKQDR 395
Cdd:TIGR02169  748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLReiEQKLNRL 824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   396 TAEGQALSEARKHLKE---ETQLRL-DVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFK 471
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEqriDLKEQIkSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   472 LQssdlgvKQKSELNsRLEEKTNQMAATIKQLEQRLRQAErsrqsaeldnRLFKQDFGDKINSLQLEVEELTRQRNQLEL 551
Cdd:TIGR02169  905 IE------ELEAQIE-KKRKRLSELKAKLEALEEELSEIE----------DPKGEDEEIPEEELSLEDVQAELQRVEEEI 967

                   .
gi 767931421   552 E 552
Cdd:TIGR02169  968 R 968
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
210-283 2.97e-05

RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A.


Pssm-ID: 439052  Cd Length: 209  Bit Score: 45.39  E-value: 2.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767931421 210 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 283
Cdd:cd17690  130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVDY-FC 203
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
316-518 2.98e-05

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 46.94  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 316 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESsyilesnrkgpkQDR 395
Cdd:COG4372   82 QLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQA------------QDL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 396 TAEGQALSEARKHLKEETQLRLDVEKELEMQISM----RQEMELAMKMLE---KDVCEKQDALVSLRQQLDDLRALKHEL 468
Cdd:COG4372  150 QTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQlksqVLDLKLRSAQIEqeaQNLATRANAAQARTEELARRAAAAQQT 229
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767931421 469 AFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAE 518
Cdd:COG4372  230 AQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLE 279
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
324-512 3.03e-05

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 46.94  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 324 KNYVEElNRHLNATVNNLQAKVDALEKSNTKLteelavaNNRIITLQEEMERVKEESSYIleSNRKGPKQDRTAEGQALS 403
Cdd:COG4372  154 KTLAEQ-RRQLEAQAQSLQASQKQLQASATQL-------KSQVLDLKLRSAQIEQEAQNL--ATRANAAQARTEELARRA 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 404 EARKHLKEETQLRLDVEKELEMQISMRQEmelamkmlekDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS-DLGVKQK 482
Cdd:COG4372  224 AAAQQTAQAIQQRDAQISQKAQQIAARAE----------QIRERERQLQRLETAQARLEQEVAQLEAYYQAYvRLRQQAA 293
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767931421 483 SELNSRLE----EKTNQMAATIKQLEQRLRQAER 512
Cdd:COG4372  294 ATQRGQVLagaaQRVAQAQAQAQAQAQLLSSANR 327
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-555 3.19e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   314 DGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKGPKQ 393
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE----LEELESRLEE 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   394 DRTAEGQALSEARKHLKEETQLRLDV---EKELEMQISMRQEM-----ELAMKMLEKDVCEkqdalvsLRQQLDDLRALK 465
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIerlEARLERLEDRRERLqqeieELLKKLEEAELKE-------LQAELEELEEEL 449
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   466 HELafklqssdlgVKQKSELNSRLEEKTNQmaatIKQLEQRLRQAErsRQSAELDNRLfkqdfgDKINSLQLEVEELTRQ 545
Cdd:TIGR02168  450 EEL----------QEELERLEEALEELREE----LEEAEQALDAAE--RELAQLQARL------DSLERLQENLEGFSEG 507
                          250
                   ....*....|
gi 767931421   546 RNQLELELKQ 555
Cdd:TIGR02168  508 VKALLKNQSG 517
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
613-648 3.28e-05

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: 41.99  E-value: 3.28e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767931421 613 CKNCSGTFCDACSTNELPLPS-SIKLE-RVCNPCHKHL 648
Cdd:cd15720   24 CRACGQVFCGKCSSKSSTIPKfGIEKEvRVCDPCYEKL 61
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
322-610 3.78e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.74  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  322 DQKNYVEELNRHLNAT---VNNLQAKVDAL-----EKSNT---------KLTEE--------------LAVANNRIITLQ 370
Cdd:pfam10174 321 DCKQHIEVLKESLTAKeqrAAILQTEVDALrlrleEKESFlnkktkqlqDLTEEkstlageirdlkdmLDVKERKINVLQ 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  371 EEMERVKE---ESSYILESNR---KGPKQDRTAEGQALSEARKHL--KEETQLRLDVEKELEMQI------SMRQEMELA 436
Cdd:pfam10174 401 KKIENLQEqlrDKDKQLAGLKervKSLQTDSSNTDTALTTLEEALseKERIIERLKEQREREDRErleeleSLKKENKDL 480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  437 ---MKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEektnqmaatiKQLEQRLRQAERS 513
Cdd:pfam10174 481 kekVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLE----------NQLKKAHNAEEAV 550
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  514 RQSAELDNRL--FKQD---FGDKINSLQLEVEELTRQRNQLELElKQEKERRLQNDRSIPGRgSQKSESKMDG--KHKMQ 586
Cdd:pfam10174 551 RTNPEINDRIrlLEQEvarYKEESGKAQAEVERLLGILREVENE-KNDKDKKIAELESLTLR-QMKEQNKKVAniKHGQQ 628
                         330       340
                  ....*....|....*....|....
gi 767931421  587 EENVKLKKPLEESHRLQPHPMDEQ 610
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNLADNS 652
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
327-561 3.82e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.02  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  327 VEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQ--DRTAEGQALSE 404
Cdd:COG1196   286 LQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLlaELEEAKEELEE 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  405 ARKHLKEETQLRLDVEKElEMQISMRQEMELAMKM--LEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK 482
Cdd:COG1196   366 KLSALLEELEELFEALRE-ELAELEAELAEIRNELeeLKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEEL 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  483 SELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAEldnrlfkqdfgDKINSLQLEVEEL--TRQRNQLELELKQEKERR 560
Cdd:COG1196   445 NEELEELEEQLEELRDRLKELERELAELQEELQRLE-----------KELSSLEARLDRLeaEQRASQGVRAVLEALESG 513

                  .
gi 767931421  561 L 561
Cdd:COG1196   514 L 514
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
613-648 5.08e-05

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: 41.62  E-value: 5.08e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSIKLERVCNPCHKHL 648
Cdd:cd15730   28 CRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL 63
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
613-644 5.14e-05

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: 41.42  E-value: 5.14e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSIKLE--RVCNPC 644
Cdd:cd15732   27 CRNCGNVFCGSCCNQKLPVPSQQLFEpsRVCKSC 60
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
316-593 5.24e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 46.63  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  316 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilESNRKgpkqdr 395
Cdd:COG1196   268 EIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEK-----IEALK------ 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  396 taegQALSEARKHLKEETQLRLDVEKELEmqiSMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 475
Cdd:COG1196   337 ----EELEERETLLEELEQLLAELEEAKE---ELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESL 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  476 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAEldnrlfkqdfgDKINSLQLEVEELTRQRNQLELELkQ 555
Cdd:COG1196   410 EERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELE-----------EQLEELRDRLKELERELAELQEEL-Q 477
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767931421  556 EKERRLQNDRSIPGRGSQKSESKMDGKHKMQEENVKLK 593
Cdd:COG1196   478 RLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLP 515
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
613-644 7.37e-05

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: 41.18  E-value: 7.37e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSI--KLERVCNPC 644
Cdd:cd15731   30 CRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
327-506 8.01e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 45.60  E-value: 8.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 327 VEELNRHLNATVNNL----QAKVDA---LEKSNTKLTEELAVANNRIITLQEEMERVKEesSYIL-----ESNRKGPKQ- 393
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREVKArkyVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTLneselESVRQLEKQl 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 394 -----------DRTAEG-QALSEARKHLKE-ETQLRlDVEKElemQISMRQEmelaMKMLEKDvcEKQdalvsLRQQLDD 460
Cdd:PRK04778 358 eslekqydeitERIAEQeIAYSELQEELEEiLKQLE-EIEKE---QEKLSEM----LQGLRKD--ELE-----AREKLER 422
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767931421 461 LRALKHELAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 506
Cdd:PRK04778 423 YRNKLHEIKRYLEKSNLpGLPE--DYLEMFFEVSDEIEALAEELEEK 467
mukB PRK04863
chromosome partition protein MukB;
402-568 8.16e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  402 LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 479
Cdd:PRK04863  444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  480 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAERsRQSAELDNRLFKQDF----GDKINSLQLEVEELTRQRNQLELELK 554
Cdd:PRK04863  519 RMRlSELEQRLRQQ--------QRAERLLAEFCK-RLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589
                         170
                  ....*....|....
gi 767931421  555 QEKERRLQNDRSIP 568
Cdd:PRK04863  590 QLQARIQRLAARAP 603
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
395-594 8.81e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.86  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  395 RTAEGQALSEARKHLKEETQLRLDVEKELEMQISM----RQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 470
Cdd:COG1196   665 QKRELKELEEELAELEAQLEKLEEELKSLKNELRSledlLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEE 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  471 KLQSsdlGVKQKSELNSRLEEKTNQMAAT---IKQLEQRLRQAERSRQS----------AELDNRLFKQDFGDKINSLQL 537
Cdd:COG1196   745 ELEE---LEEELEELQERLEELEEELESLeeaLAKLKEEIEELEEKRQAlqeeleeleeELEEAERRLDALERELESLEQ 821
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  538 EVEELTRQRNQLELELKQEKERRLQNDRSIPGRGSQKSESKMDGKH---KMQEENVKLKK 594
Cdd:COG1196   822 RRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEEleaEKEELEDELKE 881
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
320-566 9.06e-05

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


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 46.03  E-value: 9.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  320 ILDQKNYV-EELNRHLNATVNNLQAKVDaLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDRTAE 398
Cdd:COG3096   263 ISEATNYVaADYMRHANERRVHLDQALE-FRRELYTSRQQLAAEQYRHVDMSRELAELNGAEG-DLEADYQAASDHLNLV 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  399 GQALSEARKHLK-----EETQLRLDVEKELEMQISMRQ-EMELAMKMLEKDVCEKQDALVSLRQQLD--DLRALKHELAF 470
Cdd:COG3096   341 QTALRQQEKIERyqadlEELTIRLEEQNEVVEEANERQeENEARAEAAELEVDELKSQLADYQQALDvqQTRAIQYQQAI 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  471 K--------LQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKINSLQLEV-EE 541
Cdd:COG3096   421 AalerakelCHLPDLTADSAEEWLETFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAGELARSEAWDVaRE 500
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767931421  542 LTR----QRNQLE----LELKQ-EKERRLQNDRS 566
Cdd:COG3096   501 LLRegpdQRHLAEqvqpLRMRLsELEQRLRQQQS 534
CwlO1 COG3883
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
316-517 1.07e-04

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


Pssm-ID: 226400 [Multi-domain]  Cd Length: 265  Bit Score: 44.32  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 316 QITAILDQknyVEELNrhlnATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEM-ERVK------EESSY---ILE 385
Cdd:COG3883   53 EIESLDNQ---IEEIQ----SKIDELQKEIDQSKAEIKKLQKEIAELKENIVERQELLkKRARamqvngTATSYidvILN 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 386 SNRKGPKQDR-TAEGQALSEARKHLK--EETQLRL-----DVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ 457
Cdd:COG3883  126 SKSFSDLISRvTAISVIVDADKKILEqqKEDKKSLeekqaALEDKLETLVALQNELETQLNSLNSQKAEKNALIAALAAK 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767931421 458 LDDLRALKHELafklqssdlgVKQKS-ELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSA 517
Cdd:COG3883  206 EASALGEKAAL----------EEQKAlAEAAAAEAAKQEAAAKAAAQEQAALQAAATAAQP 256
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
325-542 1.22e-04

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 44.81  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 325 NYVEELNRHLNATVNNLQAKVDaLEKSNTKLTEELAvANNRIITLQEEMERVKE-ESSYILESNRKGPKQDRTAEGQALS 403
Cdd:COG4487    2 KEIKVPIQTKPFTIPKCEDSIK-GEQARYKQIEQED-QSRILNTLEEFEKEANEkRAQYRSAKKKELSQLEEQLINQKKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 404 EARKHLKEETQLRLDVEKE---LEMQISMRQEMELAMKMLEKDVCEKQDALVSL-----------RQQLDDLRALKHELA 469
Cdd:COG4487   80 QKNLFNEQIKQFELALQDEiakLEALELLNLEKDKELELLEKELDELSKELQKQlqntaeiiekkRENNKNEERLKFENE 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767931421 470 FKLQSSDLGVKQKselnsrLEEKTNQMAATIKQLEQRlRQAERSRQSAELDNRLFKQDFgdkiNSLQLEVEEL 542
Cdd:COG4487  160 KKLEESLELEREK------FEEQLHEANLDLEFKENE-EQRESKWAILKKLKRRAELGS----QQVQGEALEL 221
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2-100 1.39e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   2 AETPPPPTAGAESCSEEPARGGewRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFflLYPGDGGAGFGVRP 81
Cdd:PRK07764 598 EGPPAPASSGPPEEAARPAAPA--APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAV--PDASDGGDGWPAKA 673
                         90
                 ....*....|....*....
gi 767931421  82 PPQQQRSWRTPPSPGSPLP 100
Cdd:PRK07764 674 GGAAPAAPPPAPAPAAPAA 692
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
328-563 1.50e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 328 EELNRHLNATVNNLQAKVDALEKSntklTEELAVANNRIITLQEEMERVKEESSYIL-ESNRKGPKQDRTAEGQaLSEAR 406
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLkELEELGFESVEELEER-LKELE 598
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 407 KHLKEETQLRlDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKlqssdlgvkqkseln 486
Cdd:PRK03918 599 PFYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--------------- 662
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767931421 487 sRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFgDKINSLQLEVEELTRQRNQLElELKqEKERRLQN 563
Cdd:PRK03918 663 -ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL-EEREKAKKELEKLEKALERVE-ELR-EKVKKYKA 735
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
316-602 1.52e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   316 QITAILDQknyvEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILesnrkgpkQDR 395
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA--------QCE 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   396 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEME---LAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL 472
Cdd:TIGR00618  455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   473 QSSDLGVKQKSELNSRLEEKTNQmAATIKQLEQRLRQAE------RSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQR 546
Cdd:TIGR00618  535 QTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFsiltqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767931421   547 NQLELELKQEKerrlQNDRSIPGRGSQKSESKMDGK-HKMQEENVKLKKPLEESHRL 602
Cdd:TIGR00618  614 QHALLRKLQPE----QDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALS 666
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
338-562 2.28e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 44.36  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  338 VNNLQAKVDALEKSNTKL-------TEELAVANNRIITLQEEMERVKEE---SSYILESNRKG---------PKQDRTAE 398
Cdd:pfam07111 164 LSSLTSKAEGLEKSLNSLetkrageAKQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYvgeqvppevHSQTWELE 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  399 GQALSEARKHLKEEtqlRLDVEKELEM-QISMR--------QEMELAMKMLEKDVCEKQDALvSLRQQLDDLRALKHELA 469
Cdd:pfam07111 244 RQELLDTMQHLQED---RADLQATVELlQVRVQslthmlalQEEELTRKIQPSDSLEPEFPK-KCRSLLNRWREKVFALM 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  470 FKLQSSDLgvkqkselnsrleektnQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKinSLQLEVEELTRQRNQL 549
Cdd:pfam07111 320 VQLKAQDL-----------------EHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDK--AAEVEVERMSAKGLQM 380
                         250
                  ....*....|...
gi 767931421  550 ELELKQEKERRLQ 562
Cdd:pfam07111 381 ELSRAQEARRRQQ 393
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
372-515 2.42e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  372 EMERVKEES---SYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQ 448
Cdd:pfam17380 447 EMERVRLEEqerQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767931421  449 DALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQKSELNSRLE--EKTNQMAATIKQLEQRLRQAERSRQ 515
Cdd:pfam17380 527 KAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKATEERSRLEamEREREMMRQIVESEKARAEYEATTP 596
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
328-557 2.59e-04

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


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 44.32  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   328 EELNRHLNATVNNLQA----KVDALEKSNTKLtEELavannRIITLQEEmeRVKEESSYIL-----ESNRKGPKQDRTAE 398
Cdd:pfam15921  141 EDLRNQLQNTVHELEAakclKEDMLNDSNTQI-EQL-----RKMMLSHE--GVLQEIRSILvdfeeASGKKIYEHDSMST 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   399 ------GQALSEARKHLKEETQLR----LDVEKELEMQISMRQ-EMELAMKM----LEKDVCEKQDALVSLRQQLDDLRA 463
Cdd:pfam15921  213 ihfrslGSAISKILRELDTEISYLkgriFPVEDQLEALKSESQnKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARS 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   464 LKHELAFKLQssdLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSA--ELDNRL----------------FK 525
Cdd:pfam15921  293 QANSIQSQLE---IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKieELEKQLvlanseltearterdqFS 369
                          250       260       270
                   ....*....|....*....|....*....|..
gi 767931421   526 QDFGDKINSLQLEVEELTRQRNQLELELKQEK 557
Cdd:pfam15921  370 QESGNLDDQLQKLLADLHKREKELSLEKEQNK 401
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
613-644 2.88e-04

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: 39.24  E-value: 2.88e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 767931421 613 CKNCSGTFCDACSTNELPLPSS--IKLERVCNPC 644
Cdd:cd15734   27 CRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
PHA03264 PHA03264
envelope glycoprotein D; Provisional
3-100 2.92e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 43.84  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   3 ETPPPPTAGAescseePARGGEWRPeEPRRAPAGGTD----REGEAGPPPASPAGQ--SEPDSPVAAPFFLLYPGDGGAG 76
Cdd:PHA03264 265 EPPPAPSGGS------PAPPGDDRP-EAKPEPGPVEDgapgRETGGEGEGPEPAGRdgAAGGEPKPGPPRPAPDADRPEG 337
                         90       100
                 ....*....|....*....|....
gi 767931421  77 FgvrppPQQQRSWRTPPSPGSPLP 100
Cdd:PHA03264 338 W-----PSLEAITFPPPTPATPAV 356
PHA03247 PHA03247
large tegument protein UL36; Provisional
5-100 3.31e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421    5 PPPPTAGAESCSEEPARGGEWRP--EEPRRAPAGGTDREGEAGPPPASPAGQSEPD---SPVAAPffllyPGDGGAGFGV 79
Cdd:PHA03247 2625 DPPPPSPSPAANEPDPHPPPTVPppERPRDDPAPGRVSRPRRARRLGRAAQASSPPqrpRRRAAR-----PTVGSLTSLA 2699
                          90       100
                  ....*....|....*....|...
gi 767931421   80 RPPPQQQRSWRTPP--SPGSPLP 100
Cdd:PHA03247 2700 DPPPPPPTPEPAPHalVSATPLP 2722
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
353-565 3.38e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 3.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   353 TKLTEELAVANNRIITLQEEMERVKEessyIL-ESNRKGPKQDRTAEgqaLSEARKHLKEE-TQLRLDVE-KELEMQISM 429
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLED----ILnELERQLKSLERQAE---KAERYKELKAElRELELALLvLRLEELREE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   430 RQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLE-------EKTNQMAATIKQ 502
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkqilrERLANLERQLEE 320
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767931421   503 LEQRLRQAERSRQSAELDnrlfKQDFGDKINSLQLEVEELtRQRNQLELELKQEKERRLQNDR 565
Cdd:TIGR02168  321 LEAQLEELESKLDELAEE----LAELEEKLEELKEELESL-EAELEELEAELEELESRLEELE 378
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
613-645 3.81e-04

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: 38.95  E-value: 3.81e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSIKLE--RVCNPCH 645
Cdd:cd15733   26 CRNCGNVFCADCSNYKLPIPDEQLYDpvRVCNSCY 60
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
613-645 3.88e-04

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: 38.82  E-value: 3.88e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSI---KLERVCNPCH 645
Cdd:cd15760   24 CRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
PRK12704 PRK12704
phosphodiesterase; Provisional
480-563 5.86e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 5.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 480 KQKSELNSRLEEKTNQmaatIKQLEQRLRQAER--SRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRNQLElELKQEK 557
Cdd:PRK12704  68 KLRNEFEKELRERRNE----LQKLEKRLLQKEEnlDRKLELLEKR--EEELEKKEKELEQKQQELEKKEEELE-ELIEEQ 140

                 ....*.
gi 767931421 558 ERRLQN 563
Cdd:PRK12704 141 LQELER 146
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
322-562 5.95e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   322 DQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKgPKQDRTAEGQA 401
Cdd:pfam02463  744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK-EEAELLEEEQL 822
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   402 LSEARKHLKEETQLRLDVEKELEM--QISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFK----LQSS 475
Cdd:pfam02463  823 LIEQEEKIKEEELEELALELKEEQklEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKekeeKKEL 902
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   476 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQD---FGDKINSLQLEVEELTRQRNQLELE 552
Cdd:pfam02463  903 EEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNkeeEEERNKRLLLAKEELGKVNLMAIEE 982
                          250
                   ....*....|
gi 767931421   553 LKQEKERRLQ 562
Cdd:pfam02463  983 FEEKEERYNK 992
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
330-510 5.98e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 43.12  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  330 LNRHLNATVNNLQAKVDALEK--SNTKLTEELAVANNRII----TLQEEMERVKEESSYI----------------LESN 387
Cdd:PRK10929   80 LSAELRQQLNNERDEPRSVPPnmSTDALEQEILQVSSQLLeksrQAQQEQDRAREISDSLsqlpqqqtearrqlneIERR 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  388 RKGPKQDRTAEGQALSEARKhlKEETQLRLDVEkELEM-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDDLRA 463
Cdd:PRK10929  160 LQTLGTPNTPLAQAQLTALQ--AESAALKALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQ 236
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767931421  464 LKHELAFKL------QSSDL--GVKQKSELNSRLEEKTNQMAATIKQLEQRLRQA 510
Cdd:PRK10929  237 REAERALEStellaeQSGDLpkSIVAQFKINRELSQALNQQAQRMDLIASQQRQA 291
COG5281 COG5281
Phage-related minor tail protein [Mobilome: prophages, transposons];
294-601 6.38e-04

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


Pssm-ID: 227606 [Multi-domain]  Cd Length: 833  Bit Score: 43.09  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 294 GVIDFSMYLKDGNSSKGTEGDGQITAILDQKNYVEELNRHLnATVNNLQAKVDALEKSNTKLTEELavaNNRIITLQEEM 373
Cdd:COG5281  311 AMDDRTARVKENMGTLETAWDALADAAKKMWDAVLGIGRED-KQAALLAAKLAAEKLARVTAQGAL---NARLKLAQDDL 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 374 ERVKEE-SSYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVcEKQDALV 452
Cdd:COG5281  387 TQAELNyAAADQAANQEGALNAREDEAEVLSTQEERRDILKNLLADAEKRTARQEELNKALAKAKILQADKA-AKAYQED 465
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 453 SLRQQLDDLR--------------ALKHELAFKLQSSDL-GVKQKSELNSRLEEKTNQMAATIKqLEQRLRQaeRSRQSA 517
Cdd:COG5281  466 ILQREAQSRGktaaaersqeqmtaALKALLAFQQQIADLsGAKEKASDQKSLLWKAEEQYALLK-EEAKQRQ--LQEQKA 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 518 ELDnrlfkqdfgdkinsLQLEVEELTRqrnQLELELKQEKERRLQndrSIPGRGSQKSESKMDGKHKMQEENVKLKKPLE 597
Cdd:COG5281  543 LLE--------------HKKETLEYTS---QLAELLDQQADRFEL---SAQAAGSQKERGSDLYREALAQNAAALNKALN 602

                 ....
gi 767931421 598 ESHR 601
Cdd:COG5281  603 ELAA 606
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
3-107 6.74e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421    3 ETPPPPTAGAESCSEEPARGGEW-----RPEEPRRAPAGGTD-REGEAGPPP-ASPAGQSEPDSPVAAPFFLLYPGDGGA 75
Cdd:PHA03307   68 PTGPPPGPGTEAPANESRSTPTWslstlAPASPAREGSPTPPgPSSPDPPPPtPPPASPPPSPAPDLSEMLRPVGSPGPP 147
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767931421   76 GFGVRPPPQQQRSWRTPPSPGSPLPFLLLSYP 107
Cdd:PHA03307  148 PAASPPAAGASPAAVASDAASSRQAALPLSSP 179
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
612-644 7.42e-04

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


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 37.87  E-value: 7.42e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767931421 612 VCKNCSGTFCDACSTNELPL--PSSIKLERVCNPC 644
Cdd:cd15745   17 VCRLCGGVVCHSCSSEDLVLsvPDTCIYLRVCKTC 51
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
351-601 7.57e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.90  E-value: 7.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   351 SNTKLTEELAVANNriiTLQEEMERVKEESSYILESNRKGPKQDRtaegqALSEARKHLK--EETQLRLDVEKElemqis 428
Cdd:pfam12128  598 SEEELRERLDKAEE---ALQSAREKQAAAEEQLVQANGELEKASR-----EETFARTALKnaRLDLRRLFDEKQ------ 663
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   429 mrqemELAMKmLEKDVCEKQDALVSLRQQLD-DLRALKHEL-----AFKLQSSDLGVKQKSELNSRLEEKTNQMAAtIKQ 502
Cdd:pfam12128  664 -----SEKDK-KNKALAERKDSANERLNSLEaQLKQLDKKHqawleEQKEQKREARTEKQAYWQVVEGALDAQLAL-LKA 736
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   503 LEQRLRQAERSRQSA---ELDNRLFKQDF-GDKINSLQLEVEELTRQRNQLEL-ELKQEKERRLQNDRSI---PGRGSQK 574
Cdd:pfam12128  737 AIAARRSGAKAELKAletWYKRDLASLGVdPDVIAKLKREIRTLERKIERIAVrRQEVLRYFDWYQETWLqrrPRLATQL 816
                          250       260       270
                   ....*....|....*....|....*....|..
gi 767931421   575 SE-----SKMDGKHKMQEENVKLKKPLEESHR 601
Cdd:pfam12128  817 SNieraiSELQQQLARLIADTKLRRAKLEMER 848
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
332-557 7.61e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.79  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  332 RHLNATVNNLQAKVDALEKSNTKLTeelavANNRIITLqEEMERVKEESSYILE--SNRKGPKQDRTAEGQALSEARKHL 409
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELT-----AHCDKLLL-ENKELTQEASDMTLElkKHQEDIINCKKQEERMLKQIENLE 540
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  410 KEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRL 489
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767931421  490 EEKTNQMAATIKQLEQRLRQAERSRQSAeldnrlfKQDFGDKINSLQLEVEELTRQRNQLELELKQEK 557
Cdd:pfam05483 621 KKKGSAENKQLNAYEIKVNKLELELASA-------KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
342-590 9.19e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 9.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   342 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI--LESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDV 419
Cdd:TIGR00618  679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFneIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   420 EKELEMQISMRQEMEL----AMKMLEKDVCEKQDALVSLRQQLDDLRA-----LKHELAFKLQSSDLGVKQKSELNSRLE 490
Cdd:TIGR00618  759 RTEAHFNNNEEVTAALqtgaELSHLAAEIQFFNRLREEDTHLLKTLEAeigqeIPSDEDILNLQCETLVQEEEQFLSRLE 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   491 EKTNQMAATIKQLEQrlrQAERSRQSAELDNRLFK--QDFGD--KINSLQLEVEELTRQrnQLELELKQEKERRLQNDRS 566
Cdd:TIGR00618  839 EKSATLGEITHQLLK---YEECSKQLAQLTQEQAKiiQLSDKlnGINQIKIQFDGDALI--KFLHEITLYANVRLANQSE 913
                          250       260
                   ....*....|....*....|....
gi 767931421   567 IPGRGSQKSESKMDGKHKMQEENV 590
Cdd:TIGR00618  914 GRFHGRYADSHVNARKYQGLALLV 937
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
321-598 9.47e-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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 42.45  E-value: 9.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   321 LDQKNYVEELNRHLNATVNNLQAKVDA-------LEKSNTKLTEELAVANNRIITLQEEMErVKEESSYILESNRKGPK- 392
Cdd:pfam01576  649 LDAKEELERQNKQLRAEMEDLVSSKDDvgknvheLERSKRALEQQVEEMKTQLEELEDELQ-ATEDAKLRLEVNMQALKa 727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   393 ---QDRTAEGQALSEARKHLKEetQLRlDVEKELEMQISMRQEMELAMKMLEKDVCE-----------KQDALVSLRQQL 458
Cdd:pfam01576  728 qfeRDLQARDEQGEEKRRQLVK--QVR-ELEAELEDERKQRAQAVAAKKKLELDLKEleaqieaankgRDEAVKQLKKLQ 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   459 DDLRALKHELAFKLQSSDLGVKQKSELnsrlEEKTNQMAATIKQLEQRLRQAERSRQSAELDnrlfKQDFGDKINS---- 534
Cdd:pfam01576  805 AQMKDLQRELDEARASRDEIFAQSKES----EKKLKSLEAELLQLQEDLAAAERARRQAQQE----RDELAEEIASgnsg 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   535 ---LQLEVEELTRQRNQLELELKQE-------KER---------RLQNDRSIPGRGSQKSESkmdGKHKMQEENVKLKKP 595
Cdd:pfam01576  877 ksaLLDEKRRLEARIAQLEEELEEEqsntellNDRlrkltlqveQLTTELAAERSTSQKSES---ARQQLERQNKELKAK 953

                   ...
gi 767931421   596 LEE 598
Cdd:pfam01576  954 LQE 956
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
605-644 9.98e-04

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: 37.74  E-value: 9.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767931421 605 HPMDEQNVCKNCSGTF----------------CDACSTNELPLP--SSIKLERVCNPC 644
Cdd:cd15727    5 VPDKECPVCMSCKKKFdffkrrhhcrrcgkcfCSDCCSNKVPLPrmCFVDPVRVCNEC 62
Filament pfam00038
Intermediate filament protein;
344-557 1.01e-03

Intermediate filament protein;


Pssm-ID: 425436 [Multi-domain]  Cd Length: 313  Bit Score: 41.44  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  344 KVDALEKSNTKLTEELAVANNriitlQEEMERVKEESSY--ILESNRKGPKQDRTAEGQALSEaRKHLKEETQlrlDVEK 421
Cdd:pfam00038  19 KVRFLEQQNKDLETKISELRQ-----KKGAEPSRLYSLYerEIRELRRQLDTLTVERARLQLE-LDNLRLAAE---DFRQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  422 ELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDdlrALKHELAF--------------KLQSSDLGVKQKSELNS 487
Cdd:pfam00038  90 KYEDELNLRQSAEADIVGLRKDLDEATLARVDLEMKIE---SLKEELAFlkknheeevrelqsQVSDTQVNVEMDAARKL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  488 RLEEKTNQMAAtikQLEQrlrQAERSRQSAEldnRLFKQDF----------GDKINSLQLEVEELTRQRNQLELELKQEK 557
Cdd:pfam00038 167 DLTSALAEIRA---QYEE---IAEKNREEAE---EWYQSKLeelqqaaarnGDALRSAKEEITELRRQIQSLEIELQSLK 237
HEC1 COG5185
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ...
348-556 1.05e-03

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


Pssm-ID: 227512 [Multi-domain]  Cd Length: 622  Bit Score: 42.28  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 348 LEKSNTKLTEELAVANNRIIT-LQEEMERVKEESSYILEsnrkgpkqdRTAEGQALSEARKHLKEETQLRLDVEKELEMQ 426
Cdd:COG5185  247 LEDNYEPSEQELKLGFEKFVHiINTDIANLKTQNDNLYE---------KIQEAMKISQKIKTLREKWRALKSDSNKYENY 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 427 IS-MRQEMEL---AMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQ 502
Cdd:COG5185  318 VNaMKQKSQEwpgKLEKLKSEIELKEEEIKALQSNIDELHKQLRKQGISTEQFELMNQEREKLTRELDKINIQSDKLTKS 397
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767931421 503 LEQRLRQAERSRQSAEldnRLFkQDFGDKINSLQLEVEELTRQRNQLELELKQE 556
Cdd:COG5185  398 VKSRKLEAQGIFKSLE---KTL-RQYDSLIQNITRSRSQIGHNVNDSSLKINIE 447
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
3-100 1.07e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   3 ETPPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFFlLYPGDGGAGFGVRPP 82
Cdd:PRK07764 679 AAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLP-PEPDDPPDPAGAPAQ 757
                         90
                 ....*....|....*...
gi 767931421  83 PQQQRSWRTPPSPGSPLP 100
Cdd:PRK07764 758 PPPPPAPAPAAAPAAAPP 775
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
324-597 1.12e-03

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


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 41.98  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 324 KNYVEELNRH--LNATVNNLQAK--VDALEKSNTKLTEELAVANNRIITLQ----EEMERVKEESSYILESNRKGPKQDR 395
Cdd:COG4477  174 ENIEEELSQFveLTSSGDYIEARevLEEAEEHMIALRSIMERIPSLLAELQtelpGQLQDLKAGYRDMKEEGYHLEHVNI 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 396 TAEGQALSEARKHLKEE-TQLRLD-VEKELEMqisMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHE------ 467
Cdd:COG4477  254 DSRLERLKEQLVENSELlTQLELDeAEEELGL---IQEKIESLYDLLEREVEAKNVVEENLPILPDYLEKAKENnehlke 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 468 ------LAFKLQSSDLGVKQK-----SELNSRLEEKTNQMAatikqlEQRLRQAERSRQSAELDNRLfkqdfgDKINSLQ 536
Cdd:COG4477  331 eiervkESYRLAETELGSVRKfekelKELESVLDEILENIE------AQEVAYSELQDNLEEIEKAL------TDIEDEQ 398
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767931421 537 LEVEELTRQRNQLELELKQEKER---------RLQNDRSIPGRGSQKSESKMDGKHKMQEENVKL-KKPLE 597
Cdd:COG4477  399 EKVQEHLTSLRKDELEARENLERlksklheikRYMEKSNLPGLPETFLSLFFTAGHEIQDLMKELsEVPIN 469
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
345-448 1.29e-03

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 39.69  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  345 VDALEKSNtkltEELAVANNRIitlQEEMERVKEESSYILE-SNRKGPKQDRTAEGQALSEARKhLKEETQLRLDVEKEl 423
Cdd:TIGR01144  35 LASAERAK----KEAALAQKKA---QVILKEAKDEAQEIIEnANKRGSEILEEAKAEAREEREK-IKAQARAEIEAEKE- 105
                          90       100       110
                  ....*....|....*....|....*....|
gi 767931421  424 EMQISMRQE-----MELAMKMLEKDVCEKQ 448
Cdd:TIGR01144 106 QAREELRKQvadlsVLGAEKIIERNIDKQA 135
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
316-601 1.32e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  316 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKgpKQDR 395
Cdd:TIGR04523  69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ----KKENKK--NIDK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  396 TaegqaLSEARKHLKEETQLRLDVeKELEMQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDL-------------- 461
Cdd:TIGR04523 143 F-----LTEIKKKEKELEKLNNKY-NDLKKQK---EELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnlkkkiqkn 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  462 RALKHELA-FKLQSSDLGvKQKSELNSRLEEKTNQMAATIKQLEQRL-------RQAERSRQSAELDNRLFKQdFGDKIN 533
Cdd:TIGR04523 214 KSLESQISeLKKQNNQLK-DNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikKQLSEKQKELEQNNKKIKE-LEKQLN 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  534 SLQLEVEELTRQRNQ-------LELELKQEKERRLQND-----RSIPGRGSQKSESKMDGKHKmQEENVKLKKPLEESHR 601
Cdd:TIGR04523 292 QLKSEISDLNNQKEQdwnkelkSELKNQEKKLEEIQNQisqnnKIISQLNEQISQLKKELTNS-ESENSEKQRELEEKQN 370
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
324-601 1.35e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 324 KNYVEELNRHLNATvNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE-------SSYILESNRKGPKQDRT 396
Cdd:PRK03918 175 KRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvkeleelKEEIEELEKELESLEGS 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 397 AEG--QALSEARKHLkEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS 474
Cdd:PRK03918 254 KRKleEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 475 SDLGVKQKSELNSRLEEKTNQMAAtikqLEQRLRQAERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLELELK 554
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 767931421 555 QEKERRlqndrsipGRGSQKSESKMDGKHKMQEENVK---LKKPLEESHR 601
Cdd:PRK03918 409 KITARI--------GELKKEIKELKKAIEELKKAKGKcpvCGRELTEEHR 450
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
12-98 1.38e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 41.42  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  12 AESCSEEPARggewRPEEPRRAPAGGTDREGEAGPP-PASPAGQSEPD--SPVAAPFFLLYPGDGGAGFGVRPPPQQQRS 88
Cdd:PHA03201   4 ARSRSPSPPR----RPSPPRPTPPRSPDASPEETPPsPPGPGAEPPPGraAGPAAPRRRPRGCPAGVTFSSSAPPRPPLG 79
                         90
                 ....*....|
gi 767931421  89 WRTPPSPGSP 98
Cdd:PHA03201  80 LDDAPAATPP 89
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
333-518 1.56e-03

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 40.43  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 333 HLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYIlesnrkgpkqdrTAEGQALSEArkhlKEE 412
Cdd:COG1579   14 KLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQL------------ESEIQEIRER----IKR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 413 TQLRLDVEKELEMQISMRQEMELAmkmlekdvcekQDALVSLRQQLDDLRALKHELAfklqssdlgvKQKSELNSRLEEK 492
Cdd:COG1579   78 AEEKLSAVKDERELRALNIEIQIA-----------KERINSLEDELAELMEEIEKLE----------KEIEDLKERLERL 136
                        170       180
                 ....*....|....*....|....*.
gi 767931421 493 TNQMAATIKQLEQRLRQAERSRQSAE 518
Cdd:COG1579  137 EKNLAEAEARLEEEVAEIREEGQELS 162
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2-100 1.84e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   2 AETPPPPTAGAESCSEEPARGGewrpeePRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFFLLYPGDGGAGFGVRP 81
Cdd:PRK07764 393 APAAAAPSAAAAAPAAAPAPAA------AAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQP 466
                         90
                 ....*....|....*....
gi 767931421  82 PPQQQRSWRTPPSPGSPLP 100
Cdd:PRK07764 467 APAPAAAPEPTAAPAPAPP 485
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
237-559 2.11e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 41.25  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  237 SEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFCMKGEDLDSQvgvidfsmyLKDGNSSKGTEgDGQ 316
Cdd:pfam05483 281 DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ---------MEELNKAKAAH-SFV 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  317 ITAILDQKNYVEELNR----HLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLqEEMERVKEESSYILESNR---- 388
Cdd:pfam05483 351 VTEFEATTCSLEELLRteqqRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKqfek 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  389 -----KGPKQDRTAEGQA---------------LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQ 448
Cdd:pfam05483 430 iaeelKGKEQELIFLLQArekeihdleiqltaiKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAS 509
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  449 DALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAE---LDNRLFK 525
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEyevLKKEKQM 589
                         330       340       350
                  ....*....|....*....|....*....|....
gi 767931421  526 QDFGDKINSLQLEVEELTRQRNQLELELKQEKER 559
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2-97 2.24e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   2 AETPPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPfflLYPGDGGAGFGVRP 81
Cdd:PRK07764 616 AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAP---AAPPPAPAPAAPAA 692
                         90       100
                 ....*....|....*....|...
gi 767931421  82 P-------PQQQRSWRTPPSPGS 97
Cdd:PRK07764 693 PagaapaqPAPAPAATPPAGQAD 715
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
328-562 2.41e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 328 EELNRhLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSY------ILESNRKGPKQDRTAEGQA 401
Cdd:PRK02224 251 EELET-LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeAVEARREELEDRDEELRDR 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 402 LSEAR----KHLKEETQLR---LDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAlkhelAFKLQS 474
Cdd:PRK02224 330 LEECRvaaqAHNEEAESLRedaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE-----RFGDAP 404
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 475 SDLG-VKQKSEL----NSRLEEKTNQMAATIKQLEQRLRQAER----------------SRQSAELDNRlfkqdfGDKIN 533
Cdd:PRK02224 405 VDLGnAEDFLEElreeRDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegSPHVETIEED------RERVE 478
                        250       260       270
                 ....*....|....*....|....*....|....
gi 767931421 534 SLQLEVEELTRQRNQLE-----LELKQEKERRLQ 562
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEerlerAEDLVEAEDRIE 512
YloA COG1293
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ...
430-594 2.65e-03

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


Pssm-ID: 224212 [Multi-domain]  Cd Length: 564  Bit Score: 40.84  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 430 RQEMELAMKMLEKDVC---EKQDALVSLRQqLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQR 506
Cdd:COG1293  230 REALEELLNPLKPNYYykdEKYLDVVPLKA-YADLEKLFNEALDEKFERDKIKQLASELEKKLEKELKKLENKLEKQEDE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 507 LRQAERSrqsaelDNRLFKQdfGDKINSLQLEVEELTRQRNQLELELKQEKERRLqNDRSIPGRGSQ---KSESKMDGKH 583
Cdd:COG1293  309 LEELEKA------AEELRQK--GELLYANLQLIEEGLKSVRLADFYGNEEIKIEL-DKSKTPSENAQryfKKYKKLKGAK 379
                        170
                 ....*....|.
gi 767931421 584 KMQEENVKLKK 594
Cdd:COG1293  380 VNLDRQLSELK 390
HEC1 COG5185
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ...
328-565 2.72e-03

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


Pssm-ID: 227512 [Multi-domain]  Cd Length: 622  Bit Score: 40.74  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 328 EELNRHLNATVNNLQAKVDALEKSNTKLTeelavanNRIITLQEEMERvKEESSYILESNRKGPKQDRTAEGQALSEARK 407
Cdd:COG5185  301 REKWRALKSDSNKYENYVNAMKQKSQEWP-------GKLEKLKSEIEL-KEEEIKALQSNIDELHKQLRKQGISTEQFEL 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 408 HLKEETQLrldvEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLR--------ALKH-----------EL 468
Cdd:COG5185  373 MNQEREKL----TRELDKINIQSDKLTKSVKSRKLEAQGIFKSLEKTLRQYDSLIqnitrsrsQIGHnvndsslkiniEQ 448
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 469 AFKL----------------QSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKI 532
Cdd:COG5185  449 LFPKgsginesikksilelnDEIQERIKTEENKSITLEEDIKNLKHDINELTQILEKLELELSEANSKFELSKEENEREL 528
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767931421 533 NSLQLEVEELTRQRNQLELELKQ---EKERRLQNDR 565
Cdd:COG5185  529 VAQRIEIEKLEKELNDLNLLSKTsilDAEQLVQSTE 564
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
613-648 2.81e-03

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: 36.59  E-value: 2.81e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767931421 613 CKNCSGTFCDACSTNELPLPsSIKLE---RVCNPCHKHL 648
Cdd:cd15719   28 CRNCGQLFCSKCSRFESEIR-RLRISrpvRVCQACYNIL 65
mukB PRK04863
chromosome partition protein MukB;
328-600 2.83e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  328 EELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKeessyILesnrkgpkqDRTAEGQALSEARK 407
Cdd:PRK04863  836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLN-----LL---------ADETLADRVEEIRE 901
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  408 HLKEETQLRLDVEK------ELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ---LDDLRALKHELAFKLQSSDLG 478
Cdd:PRK04863  902 QLDEAEEAKRFVQQhgnalaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVQRRAHFSYEDAAEMLA 981
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  479 vkQKSELNSRLEEKTNQMAATIKQLEQRLRQAE-------------RSRQSAELDNRL-FKQDFGDKINSLQLEVEELTR 544
Cdd:PRK04863  982 --KNSDLNEKLRQRLEQAEQERTRAREQLRQAQaqlaqynqvlaslKSSYDAKRQMLQeLKQELQDLGVPADSGAEERAR 1059
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767931421  545 -QRNQLELELKQEKERRLQNDRSipgRGSQKSEskmdgkhkMQEENVKLKKPLEESH 600
Cdd:PRK04863 1060 aRRDELHARLSANRSRRNQLEKQ---LTFCEAE--------MDNLTKKLRKLERDYH 1105
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
323-557 3.29e-03

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


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 40.53  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   323 QKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRiitLQEEMERVKEE-------SSYI--LESNRKGPKQ 393
Cdd:pfam01576  427 QRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ---LQDTQELLQEEtrqklnlSSRLrqLEDEKNSLQE 503
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   394 DRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQ 473
Cdd:pfam01576  504 QLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRELEALTQRLEEKAAAYDKLEKTKNRLQQELD 583
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   474 SSDLGVKQKSELNSRLEEKT---NQMAATIKQLEQRlRQAERSRQSAELDNRlfkqdfGDKINSLQLEVEELTRQRNQLE 550
Cdd:pfam01576  584 DLLVDLDHQRQLVSNLEKKQkkfDQMLAEEKAISAR-YAEERDRAEAEAREK------ETKALSLARALEEALDAKEELE 656

                   ....*..
gi 767931421   551 LELKQEK 557
Cdd:pfam01576  657 RQNKQLR 663
Caldesmon pfam02029
Caldesmon;
369-588 3.73e-03

Caldesmon;


Pssm-ID: 426572 [Multi-domain]  Cd Length: 490  Bit Score: 40.24  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  369 LQEEMERVKEESSYILESN-------RKGPKQDRTAEGQALSEARK---HLKEETQLRLDVEKELEMQISMRQEMELAMK 438
Cdd:pfam02029  79 LQEALERQKELDPTITDEQaskprstENTPEEKNNTEEEEKSSTRKeryEIEEREVSEKSYEKDDKKAVPKEEEEEEDAK 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  439 MLEKDVCEKQDALVS------LRQQLDDLRALKHELAFKLQSSDLG---------VKQKSELN----SRLEEKTNQMAAT 499
Cdd:pfam02029 159 TEEEEEEEEEEKKVSkkkkekLKDEYTSKVFLDQKKGHPEQKSQNGaleevtsmtVKLKRTERtfsqKSLVAEDEEEGAA 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  500 IKQLEQRLRQAERSRQSAEldNRLFKQdFGDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDrsipgrgSQKSESKM 579
Cdd:pfam02029 239 FLEAEQKLEELRRRRQEKE--SQEFEK-LRQKQQEAELELEELKKKREERRKILEEEEQRRKQEE-------AERKAREE 308

                  ....*....
gi 767931421  580 DGKHKMQEE 588
Cdd:pfam02029 309 EEKRRMKEE 317
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
613-650 3.84e-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: 36.55  E-value: 3.84e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSIKLERVCNPCHKHLMK 650
Cdd:cd15739   29 CRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
613-645 3.97e-03

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: 36.19  E-value: 3.97e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 767931421 613 CKNCSGTFCDACSTNELPLPS-SIKLERVCNPCH 645
Cdd:cd15717   28 CRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
319-533 4.65e-03

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 40.13  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 319 AILDQKNYVEEL-NRHLNATVNNLQAKVDALEKSNTKLT---EELAVANNRIITLQEEMERVKEESSYILESNRKGPKQD 394
Cdd:COG0419  534 KLEKLENLLEELeELKEKLQLQQLKEELRQLEDRLQELKellEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLE 613
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 395 RTAEGQALSEARKHLKE---------------------ETQLRLDVEKELEMQISMRQEMELAMKMLEKDVcEKQDALVS 453
Cdd:COG0419  614 ELLQSLELSEAENELEEaeeeleseleklnlqaeleelLQAALEELEEKVEELEAEIRRELQRIENEEQLE-EKLEELEQ 692
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 454 LRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLE--QRLRQAERSRQSAELDNRLFKQDFGDK 531
Cdd:COG0419  693 LEEELEQLREELEELLKKLGEIEQLIEELESRKAELEELKKELEKLEKALEllEELREKLGKAGLRADILRNLLAQIEAE 772

                 ..
gi 767931421 532 IN 533
Cdd:COG0419  773 AN 774
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
431-580 4.91e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 38.84  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 431 QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL-----QSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQ 505
Cdd:COG1842   20 DKAEDPEKMLEQAIRDMESELAKARQALAQAIARQKQLERKLeeaqaRAEKLEEKAELALQAGNEDLAREALEEKQSLED 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931421 506 RLRQAERSRQSA-ELDNRLFKQdfgdkINSLQLEVEELTRQRNQLELELKQEKERRlQNDRSIPGRGSQKSESKMD 580
Cdd:COG1842  100 LAKALEAELQQAeEQVEKLKKQ-----LAALEQKIAELRAKKEALKARKAAAKAQE-KVNRSLGGGSSSSAMAAFE 169
PHA03378 PHA03378
EBNA-3B; Provisional
2-98 5.02e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   2 AETPPPPTAGAESCSEEPaRGGEWRPEEPRRAPAGGTDREGEAGP--PPASPAGQSEPdsPVAAPFFLLYPGDGGAGFGV 79
Cdd:PHA03378 700 APTPMRPPAAPPGRAQRP-AAATGRARPPAAAPGRARPPAAAPGRarPPAAAPGRARP--PAAAPGRARPPAAAPGAPTP 776
                         90       100
                 ....*....|....*....|....
gi 767931421  80 RPPPQ-----QQRSwRTPPSPGSP 98
Cdd:PHA03378 777 QPPPQappapQQRP-RGAPTPQPP 799
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
334-514 5.08e-03

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


Pssm-ID: 225288 [Multi-domain]  Cd Length: 652  Bit Score: 40.07  E-value: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 334 LNATVNNLQAKVDALEKSNTKLTEELAVAN-NRI-------ITLQEEMERVKEESSyilesnrkgPKQDRTAEGQALSEA 405
Cdd:COG2433  347 LAAAYKAYLAYKPKLEKVERKLPELGIWKDvERIkalvirgYPLAEALSKVKEEER---------PREKEGTEEEERREI 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 406 RKHLKEETQLRLDVEKeLEMQIsmrqemelamKMLEKDVCEKQDALVSLRQQLDDLRAlkhELAFKLQSsDLGVKQKSEL 485
Cdd:COG2433  418 TVYEKRIKKLEETVER-LEEEN----------SELKRELEELKREIEKLESELERFRR---EVRDKVRK-DREIRARDRR 482
                        170       180
                 ....*....|....*....|....*....
gi 767931421 486 NSRLEEKTNQMAATIKQLEQRLRQAERSR 514
Cdd:COG2433  483 IERLEKELEEKKKRVEELERKLAELRKMR 511
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
613-645 5.56e-03

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: 35.17  E-value: 5.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 767931421 613 CKNCSGTFCDACSTNELPLPS-SIKLERVCNPCH 645
Cdd:cd15749   18 CKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
393-559 5.87e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 39.32  E-value: 5.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 393 QDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL---- 468
Cdd:COG4942   31 FSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALevqe 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 469 ------------AFKLQSSD----LGVKQKSELNSR-----LEEKTNQMAATIKQLEQRLRQ-----AERSRQSAELDNR 522
Cdd:COG4942  111 reqrrrlaeqlaALQRSGRNpppaLLVSPEDAQRSVrlaiyYGALNPARAERIDALKATLKQlaavrAEIAAEQAELTTL 190
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767931421 523 LFKQDfgDKINSLQLEVEELTRQRNQLELELKQEKER 559
Cdd:COG4942  191 LSEQR--AQQAKLAQLLEERKKTLAQLNSELSADQKK 225
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2-98 6.09e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   2 AETPPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFFLLYPGDGGAGFGVRP 81
Cdd:PRK07764 398 APSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPT 477
                         90
                 ....*....|....*..
gi 767931421  82 PPQQQRSWRTPPSPGSP 98
Cdd:PRK07764 478 AAPAPAPPAAPAPAAAP 494
PLN02939 PLN02939
transferase, transferring glycosyl groups
342-565 6.43e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 39.89  E-value: 6.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 342 QAKVDALEKSNTKLTEELAvannriitLQEEMErvkeessyILESNrkgpkqdrtaegqaLSEARKHLKEETQLRLDVEK 421
Cdd:PLN02939 149 QARLQALEDLEKILTEKEA--------LQGKIN--------ILEMR--------------LSETDARIKLAAQEKIHVEI 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 422 ELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ----LDDLRALKHELafklqssdLGVKQKSELNSRLEEKTNQMA 497
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKAEL--------IEVAETEERVFKLEKERSLLD 270
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767931421 498 ATIKQLEQRLRQAersrQSAELDNRLFKQD-FGDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDR 565
Cdd:PLN02939 271 ASLRELESKFIVA----QEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDK 335
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
613-644 7.31e-03

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


Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 35.23  E-value: 7.31e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 767931421 613 CKNCSGTFCDACSTNELPLPSSIKLERVCNPC 644
Cdd:cd15726   26 CRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
PTZ00121 PTZ00121
MAEBL; Provisional
370-567 7.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  370 QEEMERVKEESSYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEkdvcEKQD 449
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE----DEKK 1689
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  450 ALVSLRQQLDDLRalKHELAFKLQSSDlgVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRL--FKQD 527
Cdd:PTZ00121 1690 AAEALKKEAEEAK--KAEELKKKEAEE--KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIahLKKE 1765
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767931421  528 FGDKINSLQLEVEELtrqrnqLELELKQEKE-RRLQNDRSI 567
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAV------IEEELDEEDEkRRMEVDKKI 1800
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
334-507 7.84e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 426264 [Multi-domain]  Cd Length: 170  Bit Score: 37.64  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  334 LNATVNNLQAKVDAL-EKSNTKLTEELAVANNRiitLQEEMERVKEESsyilesnrkgpkQDRTAE-----GQALSEARK 407
Cdd:pfam01442   4 LSTYAEELQEQLGPVaQELVDRLEKETEALRER---LQKDLEEVRAKL------------EPYLEElqaklQQNVEELRQ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  408 HLKEETQ-LRLDVEKELE-MQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDD-----LRALKHELAFKLQSSdlgvk 480
Cdd:pfam01442  69 RLEPYTEeLRKRLNADAEeLQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQklaerLEELKESLAPYAEEV----- 143
                         170       180
                  ....*....|....*....|....*..
gi 767931421  481 qKSELNSRLEEKTNQMAATIKQLEQRL 507
Cdd:pfam01442 144 -QAQLSQRLQELREKLEPQAEDLREKL 169
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
342-516 7.99e-03

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 39.24  E-value: 7.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 342 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESnrkgpKQDRTAEGQALSEARKHLKEEtqlRLDVEK 421
Cdd:COG4372  122 RQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQLEAQ-----AQSLQASQKQLQASATQLKSQ---VLDLKL 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 422 ELEmQISmRQEMELAMKmlEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIK 501
Cdd:COG4372  194 RSA-QIE-QEAQNLATR--ANAAQARTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQA 269
                        170
                 ....*....|....*
gi 767931421 502 QLEQRLRQAERSRQS 516
Cdd:COG4372  270 RLEQEVAQLEAYYQA 284
46 PHA02562
endonuclease subunit; Provisional
323-560 8.06e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 8.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 323 QKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMErvkeessyilesnrkgpkqDRTAEGQAL 402
Cdd:PHA02562 200 YNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE-------------------DPSAALNKL 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 403 SEARKHLKEETQLrldVEKELEM------------QISMRQEMelamkmlekdVCEKQDALVSLRQQLDDLRALKHELAF 470
Cdd:PHA02562 261 NTAAAKIKSKIEQ---FQKVIKMyekggvcptctqQISEGPDR----------ITKIKDKLKELQHSLEKLDTAIDELEE 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421 471 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQrlRQAERSRQSAEldnrlfKQDFGDKINSLQLEVEELTRQRNqle 550
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKK--VKAAIEELQAE------FVDNAEELAKLQDELDKIVKTKS--- 396
                        250
                 ....*....|
gi 767931421 551 lELKQEKERR 560
Cdd:PHA02562 397 -ELVKEKYHR 405
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
327-561 9.15e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 9.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  327 VEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMervkeessYILESNRKGPKQDRTAEGQALSEAR 406
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD--------SVKELIIKNLDNTRESLETQLKVLS 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  407 KHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS--SDLgVKQKSE 484
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDleDEL-NKDDFE 553
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421  485 LN-SRLEEKTNQMAATIKQLEQRLRQAERSRQsaELDNRLfkQDFGDKINSLQLEVEELTRQRNQLELELK--QEKERRL 561
Cdd:TIGR04523 554 LKkENLEKEIDEKNKEIEELKQTQKSLKKKQE--EKQELI--DQKEKEKKDLIKEIEEKEKKISSLEKELEkaKKENEKL 629
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1-98 9.74e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 9.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931421   1 MAETPPPPTAGAESCSEEPARGGEWRP-----EEPRRAPAGGtdREGEAGPPPASPAGQSEPDSPVAAPFFLLYPGDGGA 75
Cdd:PRK07764 683 PAPAPAAPAAPAGAAPAQPAPAPAATPpagqaDDPAAQPPQA--AQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760
                         90       100
                 ....*....|....*....|...
gi 767931421  76 GFGVRPPPQQQRSwrTPPSPGSP 98
Cdd:PRK07764 761 PPAPAPAAAPAAA--PPPSPPSE 781
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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