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Conserved domains on  [gi|19923899|ref|NP_612372|]
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centrosomal protein of 95 kDa isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF5745 pfam19016
Domain of unknown function (DUF5745); This is a domain of unknown function found in ...
51-107 2.93e-24

Domain of unknown function (DUF5745); This is a domain of unknown function found in Platyhelminthes. It shows homology with the calponin homology (CH) domain.


:

Pssm-ID: 465945  Cd Length: 59  Bit Score: 96.10  E-value: 2.93e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 19923899    51 LIVIPRSQEDDAHNVQAVIDSLALDYLQVSLSHITGENIVKGDKESIKNLLEIFDGL 107
Cdd:pfam19016   3 VIRNPSSVEDRIHNIQAVIDSLANDVLNVDLSHITPEDIVDGDPEAIRNLLEIFVGI 59
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
587-805 7.85e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 7.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    587 WKQQIAQVEQLKKEACRENRSKKKLQDEI---EEALRRHDLLTTLVKKEYEH-NKRLQDFKdcIRRQRLTQSK--IKENR 660
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALA--NEISRLEQQKqiLRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    661 QQIVRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFE-----EGLNIQKQRLRDLRNYAKEKRDEQRRRHQ---DELDSM 732
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    733 EN----------YYKDQFSLLAEAISQEHQELKAREKSQAQtlhKVKRELRSKMEKEIQQLQDMITQNDDDVFFRELEAE 802
Cdd:TIGR02168  392 ELqiaslnneieRLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELEEELEELQEELERLEEALEELRE 468

                   ...
gi 19923899    803 RFR 805
Cdd:TIGR02168  469 ELE 471
 
Name Accession Description Interval E-value
DUF5745 pfam19016
Domain of unknown function (DUF5745); This is a domain of unknown function found in ...
51-107 2.93e-24

Domain of unknown function (DUF5745); This is a domain of unknown function found in Platyhelminthes. It shows homology with the calponin homology (CH) domain.


Pssm-ID: 465945  Cd Length: 59  Bit Score: 96.10  E-value: 2.93e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 19923899    51 LIVIPRSQEDDAHNVQAVIDSLALDYLQVSLSHITGENIVKGDKESIKNLLEIFDGL 107
Cdd:pfam19016   3 VIRNPSSVEDRIHNIQAVIDSLANDVLNVDLSHITPEDIVDGDPEAIRNLLEIFVGI 59
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
587-805 7.85e-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: 7.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    587 WKQQIAQVEQLKKEACRENRSKKKLQDEI---EEALRRHDLLTTLVKKEYEH-NKRLQDFKdcIRRQRLTQSK--IKENR 660
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALA--NEISRLEQQKqiLRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    661 QQIVRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFE-----EGLNIQKQRLRDLRNYAKEKRDEQRRRHQ---DELDSM 732
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    733 EN----------YYKDQFSLLAEAISQEHQELKAREKSQAQtlhKVKRELRSKMEKEIQQLQDMITQNDDDVFFRELEAE 802
Cdd:TIGR02168  392 ELqiaslnneieRLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELEEELEELQEELERLEEALEELRE 468

                   ...
gi 19923899    803 RFR 805
Cdd:TIGR02168  469 ELE 471
PTZ00121 PTZ00121
MAEBL; Provisional
593-803 4.46e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   593 QVEQLKKEAcRENRSKKKLQDEIEEALRRHDLLttlvKKEYEHNKRLQDFKDCIRRQRLTQSKIKENRQQIVRARKYYDD 672
Cdd:PTZ00121 1471 KADEAKKKA-EEAKKADEAKKKAEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   673 YRVQLCAKMMRMRTREEmifKKLFEeglniQKQRLRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQFSLLAEAISQEHQ 752
Cdd:PTZ00121 1546 KKADELKKAEELKKAEE---KKKAE-----EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19923899   753 E-LKAREKSQAQTLHKVKRELRSKMEKEIQQLQDMITQNDDDVFFRELEAER 803
Cdd:PTZ00121 1618 AkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
584-793 5.57e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.98  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   584 SKMWKQQIAQVEQLKKEACRENRSkkklQDEIEEALRRHDLLTTLVKKEYEHNKRLQdFKDCIRRQrltqskIKENRQQI 663
Cdd:pfam13868  21 NKERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEEEEEKEEERKEERKR-YRQELEEQ------IEEREQKR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   664 VRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFEEglniqKQRLRDLRNYAKEKRDEQRRRHQDEldsmenyykdqfSLL 743
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKELEKEE------------ERE 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 19923899   744 AEAISQEHQELKAREKsqaQTLHKVKRELRSKMEKEIQQLQDMITQNDDD 793
Cdd:pfam13868 153 EDERILEYLKEKAERE---EEREAEREEIEEEKEREIARLRAQQEKAQDE 199
COG3547 COG3547
Transposase [Mobilome: prophages, transposons];
641-813 1.89e-03

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442768 [Multi-domain]  Cd Length: 349  Bit Score: 41.44  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 641 DFKDCI------RRQRLTQSKIKENRQQ----IVRARKyyddyrvqlcaKMMRMRTREemifkklfeeglniqKQRLRDL 710
Cdd:COG3547 100 DRIDAEaiaraaRRGRLRPVPVPSEEQQalraLVRRRE-----------QLVKERTAL---------------KNRLRGL 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 711 RNYAKEKRDEQRRRHQD-----ELDSMENYYKDQFSLLAEAISQEHQELKAREKsqaqtlhKVKRELRSKMEKEIQQLQD 785
Cdd:COG3547 154 LLEFGIVWGPTGRALLKrllelEAESLPPALRELLRSLLERIAALEEQIKELEK-------EIEELIKQDLDEKARLLLS 226
                       170       180       190
                ....*....|....*....|....*....|....
gi 19923899 786 M-----ITQNdddVFFREL-EAERFRSRLQLASF 813
Cdd:COG3547 227 IpgigpITAA---TLLAEIgDIGRFRSARQLAAY 257
 
Name Accession Description Interval E-value
DUF5745 pfam19016
Domain of unknown function (DUF5745); This is a domain of unknown function found in ...
51-107 2.93e-24

Domain of unknown function (DUF5745); This is a domain of unknown function found in Platyhelminthes. It shows homology with the calponin homology (CH) domain.


Pssm-ID: 465945  Cd Length: 59  Bit Score: 96.10  E-value: 2.93e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 19923899    51 LIVIPRSQEDDAHNVQAVIDSLALDYLQVSLSHITGENIVKGDKESIKNLLEIFDGL 107
Cdd:pfam19016   3 VIRNPSSVEDRIHNIQAVIDSLANDVLNVDLSHITPEDIVDGDPEAIRNLLEIFVGI 59
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
587-805 7.85e-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: 7.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    587 WKQQIAQVEQLKKEACRENRSKKKLQDEI---EEALRRHDLLTTLVKKEYEH-NKRLQDFKdcIRRQRLTQSK--IKENR 660
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALA--NEISRLEQQKqiLRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    661 QQIVRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFE-----EGLNIQKQRLRDLRNYAKEKRDEQRRRHQ---DELDSM 732
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    733 EN----------YYKDQFSLLAEAISQEHQELKAREKSQAQtlhKVKRELRSKMEKEIQQLQDMITQNDDDVFFRELEAE 802
Cdd:TIGR02168  392 ELqiaslnneieRLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELEEELEELQEELERLEEALEELRE 468

                   ...
gi 19923899    803 RFR 805
Cdd:TIGR02168  469 ELE 471
PTZ00121 PTZ00121
MAEBL; Provisional
593-803 4.46e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   593 QVEQLKKEAcRENRSKKKLQDEIEEALRRHDLLttlvKKEYEHNKRLQDFKDCIRRQRLTQSKIKENRQQIVRARKYYDD 672
Cdd:PTZ00121 1471 KADEAKKKA-EEAKKADEAKKKAEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   673 YRVQLCAKMMRMRTREEmifKKLFEeglniQKQRLRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQFSLLAEAISQEHQ 752
Cdd:PTZ00121 1546 KKADELKKAEELKKAEE---KKKAE-----EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19923899   753 E-LKAREKSQAQTLHKVKRELRSKMEKEIQQLQDMITQNDDDVFFRELEAER 803
Cdd:PTZ00121 1618 AkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
584-793 5.57e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.98  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   584 SKMWKQQIAQVEQLKKEACRENRSkkklQDEIEEALRRHDLLTTLVKKEYEHNKRLQdFKDCIRRQrltqskIKENRQQI 663
Cdd:pfam13868  21 NKERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEEEEEKEEERKEERKR-YRQELEEQ------IEEREQKR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   664 VRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFEEglniqKQRLRDLRNYAKEKRDEQRRRHQDEldsmenyykdqfSLL 743
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKELEKEE------------ERE 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 19923899   744 AEAISQEHQELKAREKsqaQTLHKVKRELRSKMEKEIQQLQDMITQNDDD 793
Cdd:pfam13868 153 EDERILEYLKEKAERE---EEREAEREEIEEEKEREIARLRAQQEKAQDE 199
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
609-808 6.71e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 6.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    609 KKLQDEIEEALRRHDLLTTLVKKE-YEHNKRLQDF---KDCIRRQRLT--------QSKIKENRQQIVRARKYYDdyrvQ 676
Cdd:TIGR02169  201 ERLRREREKAERYQALLKEKREYEgYELLKEKEALerqKEAIERQLASleeeleklTEEISELEKRLEEIEQLLE----E 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    677 LCAKMMRMRTREEMIFKKLFEE----------GLNIQKQRLRDL------------------RNYAKEKRDEQRRRHQ-- 726
Cdd:TIGR02169  277 LNKKIKDLGEEEQLRVKEKIGEleaeiaslerSIAEKERELEDAeerlakleaeidkllaeiEELEREIEEERKRRDKlt 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    727 DELDSMENYYKDQFSLLAEaISQEHQELKAREKSQAQTLHKVKRELRSkMEKEIQQLQDMITQNDDDVFFRELEAERFRS 806
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEE-VDKEFAETRDELKDYREKLEKLKREINE-LKRELDRLQEELQRLSEELADLNAAIAGIEA 434

                   ..
gi 19923899    807 RL 808
Cdd:TIGR02169  435 KI 436
COG3547 COG3547
Transposase [Mobilome: prophages, transposons];
641-813 1.89e-03

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442768 [Multi-domain]  Cd Length: 349  Bit Score: 41.44  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 641 DFKDCI------RRQRLTQSKIKENRQQ----IVRARKyyddyrvqlcaKMMRMRTREemifkklfeeglniqKQRLRDL 710
Cdd:COG3547 100 DRIDAEaiaraaRRGRLRPVPVPSEEQQalraLVRRRE-----------QLVKERTAL---------------KNRLRGL 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 711 RNYAKEKRDEQRRRHQD-----ELDSMENYYKDQFSLLAEAISQEHQELKAREKsqaqtlhKVKRELRSKMEKEIQQLQD 785
Cdd:COG3547 154 LLEFGIVWGPTGRALLKrllelEAESLPPALRELLRSLLERIAALEEQIKELEK-------EIEELIKQDLDEKARLLLS 226
                       170       180       190
                ....*....|....*....|....*....|....
gi 19923899 786 M-----ITQNdddVFFREL-EAERFRSRLQLASF 813
Cdd:COG3547 227 IpgigpITAA---TLLAEIgDIGRFRSARQLAAY 257
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
588-785 1.95e-03

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: 41.88  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    588 KQQIAQVEQLKKEAcRENRSKKKLQDEIEEALRRHDLLTTLVKKEYEHNKRLQDFKDCIRRQRLTqSKIKENRQQIVRAR 667
Cdd:pfam02463  166 RLKRKKKEALKKLI-EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL-DYLKLNEERIDLLQ 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899    668 KYYDDyRVQLCAKMMRMRTREEMIFK---KLFEEGLNIQKQRLRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQFSLLA 744
Cdd:pfam02463  244 ELLRD-EQEEIESSKQEIEKEEEKLAqvlKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 19923899    745 EAISQEHQELKAREKSQAQTLHKVKRELRSKMEKEIQQLQD 785
Cdd:pfam02463  323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
PTZ00121 PTZ00121
MAEBL; Provisional
589-778 3.96e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   589 QQIAQVEQLKK-EACRENRSKKKLQDEIEEALRRHDLLTTLVKKEYEHNKRLQDFKDCIRRQRLTQSKIKENRQQIVRAR 667
Cdd:PTZ00121 1549 DELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   668 KYYDDYRVQLCAKMMRMRTREEMIFKKlfEEGLNIQKQRLRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQfsllAEAI 747
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----EEAK 1702
                         170       180       190
                  ....*....|....*....|....*....|..
gi 19923899   748 SQEH-QELKAREKSQAQTLHKVKRELRSKMEK 778
Cdd:PTZ00121 1703 KAEElKKKEAEEKKKAEELKKAEEENKIKAEE 1734
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
588-811 4.67e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 588 KQQIAQVEQLKKEACRENRSKKKLQDEIEEALRRhdllttlvkkEYEHNKRLQdfkDCIRRQRLTQSKIKENRQQIVRAR 667
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAE----------EYELLAELA---RLEQDIARLEERRRELEERLEELE 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 668 KyyddyrvQLCAKMMRMRTREEMIfKKLFEEGLNIQKQR--LRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQFSLLAE 745
Cdd:COG1196 323 E-------ELAELEEELEELEEEL-EELEEELEEAEEELeeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923899 746 AISQEHQ--ELKAREKSQAQTLHKVKRELRSKMEKEIQQLQDMITQNDDDVFFRELEAERFRSRLQLA 811
Cdd:COG1196 395 AAELAAQleELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
CpxP COG3678
Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, ...
684-782 4.67e-03

Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442894 [Multi-domain]  Cd Length: 141  Bit Score: 38.42  E-value: 4.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 684 MRTREEMIFKKLFEeGLNI---QKQRLRDLRNYAKEKRDEQRRRHQDELDSM------ENYYKDQFSLLAEAISQEHQEL 754
Cdd:COG3678  28 GGPRGGRGLRRMLE-GLNLteeQRQQIRAIRQQYRKQMRALRQQLREAREELrallaaDKFDEAAVRALADKIAALRAQL 106
                        90       100       110
                ....*....|....*....|....*....|....
gi 19923899 755 -KAREKSQAQtLHKV-----KRELRSKMEKEIQQ 782
Cdd:COG3678 107 aVERAEARNQ-MYKVltpeqRAKLAELMQERGEK 139
46 PHA02562
endonuclease subunit; Provisional
588-794 7.27e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 7.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899  588 KQQIA-----QVEQLKKEACRENRSKKKLQDEIEEALRRHDLLTTLVKKEYEHNKRLQDFKDCIRRQRLTQSKIKENRQQ 662
Cdd:PHA02562 194 QQQIKtynknIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQ 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899  663 IVRARKYYDDYrvQLCAKMMRMRTREEMIFKKLFEEGLNIQKQrLRDLRNyakekrdeqrrrHQDELDSMENYYKDQ--- 739
Cdd:PHA02562 274 FQKVIKMYEKG--GVCPTCTQQISEGPDRITKIKDKLKELQHS-LEKLDT------------AIDELEEIMDEFNEQskk 338
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19923899  740 FSLLAEAISQEHQELKaREKSQAqtlhkvkrelrSKMEKEIQQLQDMITQNDDDV 794
Cdd:PHA02562 339 LLELKNKISTNKQSLI-TLVDKA-----------KKVKAAIEELQAEFVDNAEEL 381
PTZ00121 PTZ00121
MAEBL; Provisional
595-777 8.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 8.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   595 EQLKKEACRENRSKKKLQD--EIEEALRRHDLLTTLVKKEYEHNKRLQDFKDCIRRQRLTQSKIKENRQQIVRARKYYDD 672
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDarKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA 1223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899   673 YRVQLCAKMMRMRTREEMIfKKLFEEGLNIQKQRLRDLRNYAKEKRDE----QRRRHQDELDSMENYYK-DQFSLLAEAI 747
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKaDEAKKAEEKK 1302
                         170       180       190
                  ....*....|....*....|....*....|
gi 19923899   748 SQEHQELKAREKSQAQTLHKVKRELRSKME 777
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKAD 1332
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
591-814 9.96e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 9.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 591 IAQVEQLKKEACRenRSKKKLQDEIEEALRRhdllttLVKKEyehnKRLQDFKdciRRQRL--TQSKIKENRQQIVRARK 668
Cdd:COG3206 162 LEQNLELRREEAR--KALEFLEEQLPELRKE------LEEAE----AALEEFR---QKNGLvdLSEEAKLLLQQLSELES 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 669 YYDDYRVQLCAKMMRMRTREEMIFKKLFEEGLNIQKQRLRDLRNY---AKEKRDEQRRR----H------QDELDSMENY 735
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQlaeLEAELAELSARytpnHpdvialRAQIAALRAQ 306
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923899 736 YKDQFSLLAEAISQEHQELKAREKSQAQTLHKVKRELRS--KMEKEIQQLQdmitqndddvffRELEA-----ERFRSRL 808
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAElpELEAELRRLE------------REVEVarelyESLLQRL 374

                ....*.
gi 19923899 809 QLASFQ 814
Cdd:COG3206 375 EEARLA 380
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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